Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.
The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Derivatives of ammonium compounds, NH4+ Y-, in which all four of the hydrogens bonded to nitrogen have been replaced with hydrocarbyl groups. These are distinguished from IMINES which are RN=CR2.
Sequential operating programs and data which instruct the functioning of a digital computer.
A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.
A genus of facultatively anaerobic, gram-positive bacteria in the family ACTINOMYCETACEAE, order ACTINOMYCETALES. They are obligate parasites of the PHARYNX in humans and farm animals.
A field of biology concerned with the development of techniques for the collection and manipulation of biological data, and the use of such data to make biological discoveries or predictions. This field encompasses all computational methods and theories for solving biological problems including manipulation of models and datasets.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
Computer-based representation of physical systems and phenomena such as chemical processes.
A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The parts of a macromolecule that directly participate in its specific combination with another molecule.
NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.
The portion of an interactive computer program that issues messages to and receives commands from a user.
A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)
A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
The process of pictorial communication, between human and computers, in which the computer input and output have the form of charts, drawings, or other appropriate pictorial representation.
One of two groups of viruses in the ARENAVIRUS genus and considered part of the New World complex. It includes JUNIN VIRUS; PICHINDE VIRUS; Amapari virus, and Machupo virus among others. They are the cause of human hemorrhagic fevers mostly in Central and South America.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Care given to patients by nursing service personnel.
The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.
A computer simulation developed to study the motion of molecules over a period of time.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)
The thermodynamic interaction between a substance and WATER.
Liquids that dissolve other substances (solutes), generally solids, without any change in chemical composition, as, water containing sugar. (Grant & Hackh's Chemical Dictionary, 5th ed)
Devices used to support or align the foot structure, or to prevent or correct foot deformities.
The branch of science that deals with the geometric description of crystals and their internal arrangement. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The scattering of x-rays by matter, especially crystals, with accompanying variation in intensity due to interference effects. Analysis of the crystal structure of materials is performed by passing x-rays through them and registering the diffraction image of the rays (CRYSTALLOGRAPHY, X-RAY). (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The rate dynamics in chemical or physical systems.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
The accumulation of an electric charge on a object
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
Proteins found in any species of bacterium.
The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Extensive collections, reputedly complete, of facts and data garnered from material of a specialized subject area and made available for analysis and application. The collection can be automated by various contemporary methods for retrieval. The concept should be differentiated from DATABASES, BIBLIOGRAPHIC which is restricted to collections of bibliographic references.
A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC
Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.
The homogeneous mixtures formed by the mixing of a solid, liquid, or gaseous substance (solute) with a liquid (the solvent), from which the dissolved substances can be recovered by physical processes. (From Grant & Hackh's Chemical Dictionary, 5th ed)
Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
Methods for determining interaction between PROTEINS.
The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations.
Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.
A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Collections of facts, assumptions, beliefs, and heuristics that are used in combination with databases to achieve desired results, such as a diagnosis, an interpretation, or a solution to a problem (From McGraw Hill Dictionary of Scientific and Technical Terms, 6th ed).
A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
The characteristic three-dimensional shape of a molecule.
A monomeric calcium-calmodulin-dependent protein kinase subtype that is primarily expressed in neuronal tissues; T-LYMPHOCYTES and TESTIS. The activity of this enzyme is regulated by its phosphorylation by CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE.
A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
Organized activities related to the storage, location, search, and retrieval of information.
Software designed to store, manipulate, manage, and control data for specific uses.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
The relationships of groups of organisms as reflected by their genetic makeup.
Scattering of a beam of electromagnetic or acoustic RADIATION, or particles, at small angles by particles or cavities whose dimensions are many times as large as the wavelength of the radiation or the de Broglie wavelength of the scattered particles. Also know as low angle scattering. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Small angle scattering (SAS) techniques, small angle neutron (SANS), X-ray (SAXS), and light (SALS, or just LS) scattering, are used to characterize objects on a nanoscale.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
Electron microscopy involving rapid freezing of the samples. The imaging of frozen-hydrated molecules and organelles permits the best possible resolution closest to the living state, free of chemical fixatives or stains.
The study of CHEMICAL PHENOMENA and processes in terms of the underlying PHYSICAL PHENOMENA and processes.
The physical phenomena describing the structure and properties of atoms and molecules, and their reaction and interaction processes.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.
Normal adult human hemoglobin. The globin moiety consists of two alpha and two beta chains.
Proteins prepared by recombinant DNA technology.
In statistics, a technique for numerically approximating the solution of a mathematical problem by studying the distribution of some random variable, often generated by a computer. The name alludes to the randomness characteristic of the games of chance played at the gambling casinos in Monte Carlo. (From Random House Unabridged Dictionary, 2d ed, 1993)
In INFORMATION RETRIEVAL, machine-sensing or identification of visible patterns (shapes, forms, and configurations). (Harrod's Librarians' Glossary, 7th ed)
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
Statistical formulations or analyses which, when applied to data and found to fit the data, are then used to verify the assumptions and parameters used in the analysis. Examples of statistical models are the linear model, binomial model, polynomial model, two-parameter model, etc.
A mixture of alkylbenzyldimethylammonium compounds. It is a bactericidal quaternary ammonium detergent used topically in medicaments, deodorants, mouthwashes, as a surgical antiseptic, and as a as preservative and emulsifier in drugs and cosmetics.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
The systematic study of the complete complement of proteins (PROTEOME) of organisms.
Measurement of the intensity and quality of fluorescence.
The diversion of RADIATION (thermal, electromagnetic, or nuclear) from its original path as a result of interactions or collisions with atoms, molecules, or larger particles in the atmosphere or other media. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
The statistical reproducibility of measurements (often in a clinical context), including the testing of instrumentation or techniques to obtain reproducible results. The concept includes reproducibility of physiological measurements, which may be used to develop rules to assess probability or prognosis, or response to a stimulus; reproducibility of occurrence of a condition; and reproducibility of experimental results.
The quality or state of being able to be bent or creased repeatedly. (From Webster, 3d ed)
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
Proteins obtained from ESCHERICHIA COLI.
A computer architecture, implementable in either hardware or software, modeled after biological neural networks. Like the biological system in which the processing capability is a result of the interconnection strengths between arrays of nonlinear processing nodes, computerized neural networks, often called perceptrons or multilayer connectionist models, consist of neuron-like units. A homogeneous group of units makes up a layer. These networks are good at pattern recognition. They are adaptive, performing tasks by example, and thus are better for decision-making than are linear learning machines or cluster analysis. They do not require explicit programming.
Theoretical representations that simulate the behavior or activity of systems, processes, or phenomena. They include the use of mathematical equations, computers, and other electronic equipment.
The physical characteristics and processes of biological systems.
The systematic study of the complete DNA sequences (GENOME) of organisms.
The study of PHYSICAL PHENOMENA and PHYSICAL PROCESSES as applied to living things.
Devices for accelerating protons or electrons in closed orbits where the accelerating voltage and magnetic field strength varies (the accelerating voltage is held constant for electrons) in order to keep the orbit radius constant.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
The measure of that part of the heat or energy of a system which is not available to perform work. Entropy increases in all natural (spontaneous and irreversible) processes. (From Dorland, 28th ed)
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
Substances used on inanimate objects that destroy harmful microorganisms or inhibit their activity. Disinfectants are classed as complete, destroying SPORES as well as vegetative forms of microorganisms, or incomplete, destroying only vegetative forms of the organisms. They are distinguished from ANTISEPTICS, which are local anti-infective agents used on humans and other animals. (From Hawley's Condensed Chemical Dictionary, 11th ed)
Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Characteristics or attributes of the outer boundaries of objects, including molecules.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
A spectroscopic technique in which a range of wavelengths is presented simultaneously with an interferometer and the spectrum is mathematically derived from the pattern thus obtained.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Controlled operation of an apparatus, process, or system by mechanical or electronic devices that take the place of human organs of observation, effort, and decision. (From Webster's Collegiate Dictionary, 1993)
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight [1.00784; 1.00811]. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are PROTONS. Besides the common H1 isotope, hydrogen exists as the stable isotope DEUTERIUM and the unstable, radioactive isotope TRITIUM.
Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light.
Spectrophotometry in the infrared region, usually for the purpose of chemical analysis through measurement of absorption spectra associated with rotational and vibrational energy levels of molecules. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.
A non-crystalline form of silicon oxide that has absorptive properties. It is commonly used as a desiccating agent and as a stationary phase for CHROMATOGRAPHY. The fully hydrated form of silica gel has distinct properties and is referred to as SILICIC ACID.
The sum of the weight of all the atoms in a molecule.
Conformational transitions of the shape of a protein to various unfolded states.
Substances produced from the reaction between acids and bases; compounds consisting of a metal (positive) and nonmetal (negative) radical. (Grant & Hackh's Chemical Dictionary, 5th ed)
Macromolecular complexes formed from the association of defined protein subunits.
A representation, generally small in scale, to show the structure, construction, or appearance of something. (From Random House Unabridged Dictionary, 2d ed)
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Numeric or quantitative entities, descriptions, properties, relationships, operations, and events.
Computer-assisted analysis and processing of problems in a particular area.
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
An enzyme that catalyzes the endonucleolytic cleavage of pancreatic ribonucleic acids to 3'-phosphomono- and oligonucleotides ending in cytidylic or uridylic acids with 2',3'-cyclic phosphate intermediates. EC
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed)
A research technique to measure solvent exposed regions of molecules that is used to provide insight about PROTEIN CONFORMATION.
A subclass of ANTIFREEZE PROTEINS that have a cystine-rich globular structure of approximately 14 kD.
A stochastic process such that the conditional probability distribution for a state at any future instant, given the present state, is unaffected by any additional knowledge of the past history of the system.
A strong organic base existing primarily as guanidium ions at physiological pH. It is found in the urine as a normal product of protein metabolism. It is also used in laboratory research as a protein denaturant. (From Martindale, the Extra Pharmacopoeia, 30th ed and Merck Index, 12th ed) It is also used in the treatment of myasthenia and as a fluorescent probe in HPLC.
Proteins produced from GENES that have acquired MUTATIONS.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
Cationic bactericidal surfactant used as a topical antiseptic for skin, wounds, mucous membranes, instruments, etc.; and also as a component in mouthwash and lozenges.
Electrically neutral elementary particles found in all atomic nuclei except light hydrogen; the mass is equal to that of the proton and electron combined and they are unstable when isolated from the nucleus, undergoing beta decay. Slow, thermal, epithermal, and fast neutrons refer to the energy levels with which the neutrons are ejected from heavier nuclei during their decay.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The molecular designing of drugs for specific purposes (such as DNA-binding, enzyme inhibition, anti-cancer efficacy, etc.) based on knowledge of molecular properties such as activity of functional groups, molecular geometry, and electronic structure, and also on information cataloged on analogous molecules. Drug design is generally computer-assisted molecular modeling and does not include pharmacokinetics, dosage analysis, or drug administration analysis.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A non-heme iron protein consisting of eight apparently identical subunits each containing 2 iron atoms. It binds one molecule of oxygen per pair of iron atoms and functions as a respiratory protein.
The addition of descriptive information about the function or structure of a molecular sequence to its MOLECULAR SEQUENCE DATA record.
Virulent bacteriophage and type species of the genus T4-like phages, in the family MYOVIRIDAE. It infects E. coli and is the best known of the T-even phages. Its virion contains linear double-stranded DNA, terminally redundant and circularly permuted.
An atom or group of atoms that have a positive or negative electric charge due to a gain (negative charge) or loss (positive charge) of one or more electrons. Atoms with a positive charge are known as CATIONS; those with a negative charge are ANIONS.
Continuous frequency distribution of infinite range. Its properties are as follows: 1, continuous, symmetrical distribution with both tails extending to infinity; 2, arithmetic mean, mode, and median identical; and 3, shape completely determined by the mean and standard deviation.
Purifying or cleansing agents, usually salts of long-chain aliphatic bases or acids, that exert cleansing (oil-dissolving) and antimicrobial effects through a surface action that depends on possessing both hydrophilic and hydrophobic properties.
A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.
Physical motion, i.e., a change in position of a body or subject as a result of an external force. It is distinguished from MOVEMENT, a process resulting from biological activity.
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
The process of cumulative change over successive generations through which organisms acquire their distinguishing morphological and physiological characteristics.
A compound formed by the combination of hemoglobin and oxygen. It is a complex in which the oxygen is bound directly to the iron without causing a change from the ferrous to the ferric state.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC
Genotypic differences observed among individuals in a population.
PASSERIFORMES of the suborder, Oscines, in which the flexor tendons of the toes are separate, and the lower syrinx has 4 to 9 pairs of tensor muscles inserted at both ends of the tracheal half rings. They include many commonly recognized birds such as CROWS; FINCHES; robins; SPARROWS; and SWALLOWS.
A mass spectrometry technique used for analysis of nonvolatile compounds such as proteins and macromolecules. The technique involves preparing electrically charged droplets from analyte molecules dissolved in solvent. The electrically charged droplets enter a vacuum chamber where the solvent is evaporated. Evaporation of solvent reduces the droplet size, thereby increasing the coulombic repulsion within the droplet. As the charged droplets get smaller, the excess charge within them causes them to disintegrate and release analyte molecules. The volatilized analyte molecules are then analyzed by mass spectrometry.
A class of iron-sulfur proteins that contains one iron coordinated to the sulfur atom of four cysteine residues. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Particles consisting of aggregates of molecules held loosely together by secondary bonds. The surface of micelles are usually comprised of amphiphatic compounds that are oriented in a way that minimizes the energy of interaction between the micelle and its environment. Liquids that contain large numbers of suspended micelles are referred to as EMULSIONS.
The procedures involved in combining separately developed modules, components, or subsystems so that they work together as a complete system. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.
Systems where the input data enter the computer directly from the point of origin (usually a terminal or workstation) and/or in which output data are transmitted directly to that terminal point of origin. (Sippl, Computer Dictionary, 4th ed)
The theory that the radiation and absorption of energy take place in definite quantities called quanta (E) which vary in size and are defined by the equation E=hv in which h is Planck's constant and v is the frequency of the radiation.
Specific languages used to prepare computer programs.
Penetrating electromagnetic radiation emitted when the inner orbital electrons of an atom are excited and release radiant energy. X-ray wavelengths range from 1 pm to 10 nm. Hard X-rays are the higher energy, shorter wavelength X-rays. Soft x-rays or Grenz rays are less energetic and longer in wavelength. The short wavelength end of the X-ray spectrum overlaps the GAMMA RAYS wavelength range. The distinction between gamma rays and X-rays is based on their radiation source.
The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Application of statistical procedures to analyze specific observed or assumed facts from a particular study.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
Electropositive chemical elements characterized by ductility, malleability, luster, and conductance of heat and electricity. They can replace the hydrogen of an acid and form bases with hydroxyl radicals. (Grant & Hackh's Chemical Dictionary, 5th ed)
Elements of limited time intervals, contributing to particular results or situations.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
Organic compounds containing the -CO-NH2 radical. Amides are derived from acids by replacement of -OH by -NH2 or from ammonia by the replacement of H by an acyl group. (From Grant & Hackh's Chemical Dictionary, 5th ed)
Proteins found in any species of archaeon.
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
Compounds that contain the decamethylenebis(trimethyl)ammonium radical. These compounds frequently act as neuromuscular depolarizing agents.
A nonmetallic element with atomic symbol C, atomic number 6, and atomic weight [12.0096; 12.0116]. It may occur as several different allotropes including DIAMOND; CHARCOAL; and GRAPHITE; and as SOOT from incompletely burned fuel.
Stable elementary particles having the smallest known positive charge, found in the nuclei of all elements. The proton mass is less than that of a neutron. A proton is the nucleus of the light hydrogen atom, i.e., the hydrogen ion.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
A mutation in which a codon is mutated to one directing the incorporation of a different amino acid. This substitution may result in an inactive or unstable product. (From A Dictionary of Genetics, King & Stansfield, 5th ed)
A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Rhodopsins found in the PURPLE MEMBRANE of halophilic archaea such as HALOBACTERIUM HALOBIUM. Bacteriorhodopsins function as an energy transducers, converting light energy into electrochemical energy via PROTON PUMPS.
Macrocyclic polyethers with the repeating unit of (-CH2-CH2-O)n where n is greater than 2 and some oxygens may be replaced by nitrogen, sulfur or phosphorus. These compounds are useful for coordinating CATIONS. The nomenclature uses a prefix to indicate the size of the ring and a suffix for the number of heteroatoms.
The protein complement of an organism coded for by its genome.
The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Amino acids containing an aromatic side chain.
The scattering of NEUTRONS by matter, especially crystals, with accompanying variation in intensity due to interference effects. It is useful in CRYSTALLOGRAPHY and POWDER DIFFRACTION.

Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution. (1/6360)

The crystal structure of beta-amylase from Bacillus cereus var. mycoides was determined by the multiple isomorphous replacement method. The structure was refined to a final R-factor of 0.186 for 102,807 independent reflections with F/sigma(F) > or = 2.0 at 2.2 A resolution with root-mean-square deviations from ideality in bond lengths, and bond angles of 0.014 A and 3.00 degrees, respectively. The asymmetric unit comprises four molecules exhibiting a dimer-of-dimers structure. The enzyme, however, acts as a monomer in solution. The beta-amylase molecule folds into three domains; the first one is the N-terminal catalytic domain with a (beta/alpha)8 barrel, the second one is the excursion part from the first one, and the third one is the C-terminal domain with two almost anti-parallel beta-sheets. The active site cleft, including two putative catalytic residues (Glu172 and Glu367), is located on the carboxyl side of the central beta-sheet in the (beta/alpha)8 barrel, as in most amylases. The active site structure of the enzyme resembles that of soybean beta-amylase with slight differences. One calcium ion is bound per molecule far from the active site. The C-terminal domain has a fold similar to the raw starch binding domains of cyclodextrin glycosyltransferase and glucoamylase.  (+info)

Expression and characterisation of the heavy chain of tetanus toxin: reconstitution of the fully-recombinant dichain protein in active form. (2/6360)

Tetanus toxin, composed of a disulphide-linked heavy (HC) and light (LC) chain, preferentially blocks the release of inhibitory neurotransmitters in the spinal cord by Zn2+-dependent proteolytic cleavage of synaptobrevin. This intoxication involves binding via HC to ecto-acceptors on peripheral nerve endings, followed by internalisation and retrograde transportation to its prime site of action in central neurons. To facilitate exploitation of the toxin's unique activities, HC was expressed at a high level in Escherichia coli as a fusion with maltose binding protein; after cleavage by thrombin, free HC was isolated and its identity confirmed by Western blotting and N-terminal microsequencing. The expressed and native HC gave very similar circular dichroism spectra, excluding any gross differences in their folded structures. Recombinant HC antagonised the neuromuscular paralysing activity of the native toxin, by competing for binding to neuronal ecto-acceptors. The HC was reconstituted with bacterially-expressed LC to create disulphide-bridged dichain toxin that blocked neuromuscular transmission. The fully-recombinant toxin produced spastic paralysis in mice characteristic of the blockade of central inhibitory synapses, revealing that it undergoes axonal transport to the spinal cord, like the native toxin but with a reduced efficacy. This first report of the large-scale production of recombinant tetanus toxin in active form should facilitate studies on the use of engineered innocuous forms of the toxin as neuronal transport vehicles.  (+info)

The spineless-aristapedia and tango bHLH-PAS proteins interact to control antennal and tarsal development in Drosophila. (3/6360)

The Drosophila spineless (ss) gene encodes a basic-helix-loop-helix-PAS transcription factor that is required for proper specification of distal antennal identity, establishment of the tarsal regions of the legs, and normal bristle growth. ss is the closest known homolog of the mammalian aryl hydrocarbon receptor (Ahr), also known as the dioxin receptor. Dioxin and other aryl hydrocarbons bind to the PAS domain of Ahr, causing Ahr to translocate to the nucleus, where it dimerizes with another bHLH-PAS protein, the aryl hydrocarbon receptor nuclear translocator (Arnt). Ahr:Arnt heterodimers then activate transcription of target genes that encode enzymes involved in metabolizing aryl hydrocarbons. In this report, we present evidence that Ss functions as a heterodimer with the Drosophila ortholog of Arnt, Tango (Tgo). We show that the ss and tgo genes have a close functional relationship: loss-of-function alleles of tgo were recovered as dominant enhancers of a ss mutation, and tgo-mutant somatic clones show antennal, leg, and bristle defects almost identical to those caused by ss(-) mutations. The results of yeast two-hybrid assays indicate that the Ss and Tgo proteins interact directly, presumably by forming heterodimers. Coexpression of Ss and Tgo in Drosophila SL2 cells causes transcriptional activation of reporters containing mammalian Ahr:Arnt response elements, indicating that Ss:Tgo heterodimers are very similar to Ahr:Arnt heterodimers in DNA-binding specificity and transcriptional activation ability. During embryogenesis, Tgo is localized to the nucleus at sites of ss expression. This localization is lost in a ss null mutant, suggesting that Tgo requires heterodimerization for translocation to the nucleus. Ectopic expression of ss causes coincident ectopic nuclear localization of Tgo, independent of cell type or developmental stage. This suggests that the interaction of Ss and Tgo does not require additional signals, unlike the ligand-dependent interaction of Ahr and Arnt. Despite the very different biological roles of Ahr and Arnt in insects and mammals, the molecular mechanisms by which these proteins function appear to be largely conserved.  (+info)

Influence of the mu-chain C-terminal sequence on polymerization of immunoglobulin M. (4/6360)

Immunoglobulin (IgM) is found in various states of covalent polymerization (microL)n, where n is typically 8, 10, or 12. The usual form of IgM of bony fish is tetrameric (8 microL units) as compared to the pentameric form (10 microL units) observed in cartilaginous fish and mammals. Two hypotheses were tested in this study. First, that the length of the mu-chain C terminus following Cys575 determines whether an IgM polymerizes as a tetramer or as a pentamer. This was tested by examining the covalent polymerization state of mouse IgM mutated to contain a series of mu-chain C-termini from bony and cartilaginous fish. The results proved this hypothesis wrong: mouse IgM bearing the C-terminal sequence of shark, salmon and cod mu-chain behaved identically to native mouse IgM, forming predominantly (microL)10 and (microL)12 forms. The second hypothesis was that an additional Cys residue near the C terminus of the mu-chain is responsible for the multiple covalent structures seen in IgM of the channel catfish. The addition of a catfish C terminus to the mouse mu-chain resulted, as predicted, in the production of a series of covalently bonded forms, with the major species being (microL)4. When a Ser-Cys unit was removed from the catfish C terminus added to the mouse mu-chain, this resulted in production of IgM indistinguishable in structure from that of wild-type mouse IgM.  (+info)

Structural requirement of the calcium-channel subunit alpha2delta for gabapentin binding. (5/6360)

Gabapentin [Neurontin, 1-(aminomethyl)cyclohexaneacetic acid] is a novel anticonvulsant drug with a high binding affinity for the Ca(2+)-channel subunit alpha(2)delta. In this study, the gabapentin-binding properties of wild-type and mutated porcine brain alpha(2)delta proteins were investigated. Removal of the disulphide bonds between the alpha(2) and the delta subunits did not result in a significant loss of gabapentin binding, suggesting that the disulphide linkage between the two subunits is not required for binding. Singly expressed alpha(2) protein remained membrane associated. However, alpha(2) alone was unable to bind gabapentin, unless the cells were concurrently transfected with the expression vector for delta, suggesting that both alpha(2) and delta are required for gabapentin binding. Using internal deletion mutagenesis, we mapped two regions [amino acid residues 339-365 (DeltaF) and 875-905 (DeltaJ)] within the alpha(2) subunit that are not required for gabapentin binding. Further, deletion of three other individual regions [amino acid residues 206-222 (DeltaD), 516-537 (DeltaH) and 583-603 (DeltaI)] within the alpha(2) subunit disrupted gabapentin binding, suggesting the structural importance of these regions. Using alanine to replace four to six amino acid residues in each of these regions abolished gabapentin binding. These results demonstrate that region D, between the N-terminal end and the first putative transmembrane domain of alpha(2), and regions H and I, between the putative splicing acceptor sites (Gln(511) and Ser(601)), may play important roles in maintaining the structural integrity for gabapentin binding. Further single amino acid replacement mutagenesis within these regions identified Arg(217) as critical for gabapentin binding.  (+info)

Evidence that platelet and tumour heparanases are similar enzymes. (6/6360)

In order to enter tissues, blood-borne metastatic tumour cells and leucocytes need to extravasate through the vascular basal lamina (BL), a process which involves a battery of degradative enzymes. A key degradative enzyme is the endoglycosidase heparanase, which cleaves heparan sulphate (HS), an important structural component of the vascular BL. Previously, tumour-derived heparanase activity (which has been shown to be related to the metastatic potential of murine and human melanoma cell lines) was reported to cleave HS and be inhibited by heparin, as distinct from human platelet heparanase, which cleaved both substrates [Nakajima, Irimura and Nicolson (1988) J. Cell Biochem. 36, 157-167]. We recently reported the purification of human platelet heparanase and showed that the enzyme is a 50-kDa endoglucuronidase [Freeman and Parish (1998) Biochem. J. 330, 1341-1350]. We now report the purification and characterization of heparanase activity from highly metastatic rat 13762 MAT mammary adenocarcinoma and human HCT 116 colonic carcinoma cells and from rat liver using essentially the same procedure that was reported for purification of the human platelet enzyme. The rat 13762 MAT tumour enzyme, which has a native M(r) of 45 kDa when analysed by gel-filtration chromatography and by SDS/PAGE, was observed to be an endoglucuronidase that degraded heparin and HS to fragments of the same sizes as the human platelet enzyme does. N-deglycosylation of both the human platelet and rat 13762 MAT tumour enzymes gave, in each case, a 41-kDa band by SDS/PAGE analysis, demonstrating that the observed difference in M(r) between the platelet and tumour enzymes may have been due largely to differences in the relative amounts of N-glycosylation. Two peptides were isolated following Endoproteinase Lys-C digestion of both the human platelet and rat 13762 MAT tumour heparanases and were shown to be highly similar. Both the rat liver and human colonic carcinoma heparanases also degraded both heparin and HS to fragments of the same sizes as the human platelet enzyme does. Western-blot analysis of an SDS/PAGE gel using antibodies raised against human platelet heparanase demonstrated that human platelet, human tumour and rat tumour heparanases were immunochemically cross-reactive. In conclusion, because of the similarities in their sizes, substrate specificities, peptide sequences and immunoreactivities, we propose that heparanase activities present in human platelets, rat liver and in rat and human tumour cells are, in fact, mediated by a similar enzyme.  (+info)

Processing and functional display of the 86 kDa heterodimeric penicillin G acylase on the surface of phage fd. (7/6360)

The large heterodimeric penicillin G acylase from Alcaligenes faecalis was displayed on the surface of phage fd. We fused the coding sequence (alpha subunit-internal peptide-beta subunit) to the gene of a phage coat protein. A modified g3p signal sequence was used to direct the polypeptide to the periplasm. Here we show that a heterodimeric enzyme can be expressed as a fusion protein that matures to an active biocatalyst connected to the coat protein of phage fd, resulting in a phage to which the beta-subunit is covalently linked and the alpha-subunit is non-covalently attached. The enzyme can be displayed either fused to the minor coat protein g3p or fused to the major coat protein g8p. In both cases the penicillin G acylase on the phage has the same Michaelis constant as its freely soluble counterpart, indicating a proper folding and catalytic activity of the displayed enzyme. The display of the heterodimer on phage not only allows its further use in protein engineering but also offers the possibility of applying this technology for the excretion of the enzyme into the extracellular medium, facilitating purification of the protein. With the example of penicillin acylase the upper limit for a protein to become functionally displayed by phage fd has been further explored. Polyvalent display was not observed despite the use of genetic constructs designed for this aim. These results are discussed in relation to the pore size being formed by the g4p multimer.  (+info)

Receptor signaling: when dimerization is not enough. (8/6360)

Activation of receptors that signal via tyrosine kinase domains has been thought to involve receptor dimerization and transphosphorylation of juxtaposed catalytic domains. Recent results suggest things might be more complex - specific intersubunit conformational changes within a dimer can also be important.  (+info)

Quaternary structure|Quaternary state of a protein ( usually, although it can apply to other larger molecules, biological or synthetic ) where more than...
p>This subsection of the ,a href=>Interaction,/a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the ,a href=>Function,/a> section).,p>,a href=/help/subunit_structure target=_top>More...,/a>,/p>Subunit structurei ...
1wbl: Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution.
Define quaternary: of, relating to, or consisting of four units or members; of, relating to, or being a number system with a base of four
Quaternary The Cenozoic era [1], 65 million years ago to the present, is divided into two periods, the Tertiary and the Quaternary. The Tertiary period [2], 65 to 2 million years ago, encompasses the rebuilding of the animal kingdom at the end of the great Cretaceous extinction.
Quaternary Prevention: Action taken to identify patient at risk of overmedicalisation, to protect him from new medical invasion, and to suggest to him interventions, which are ethically acceptable.
Carbonic anhydrase (CA) IX is a plasma membrane-associated member of the alpha-CA enzyme family, which is involved in solid tumor acidification. It is a marker of tumor hypoxia and a prognostic factor in several human cancers. An aberrant increase in CA IX expression in chronic hypoxia and during development of various carcinomas contributes to tumorigenesis through at least two mechanisms: pH regulation and cell adhesion control. Here we report the X-ray structure of the catalytic domain of CA IX in complex with a classical, clinically used sulfonamide inhibitor, acetazolamide. The structure reveals a typical alpha-CA fold, which significantly differs from the other CA isozymes when the protein quaternary structure is considered. Thus, two catalytic domains of CA IX associate to form a dimer, which is stabilized by the formation of an intermolecular disulfide bond. The active site clefts and the PG domains are located on one face of the dimer, while the C-termini are located on the opposite ...
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In proteins, there are four recognized levels of protein structure: primary structure, secondary structure, tertiary structure, and quaternary structure. A quaternary structure of a protein refers to the assembly of multiple folded protein molecules in a multi-subunit complex. ...
KCTD21 (potassium channel tetramerization domain containing 21), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
Looking for oligomeric protein? Find out information about oligomeric protein. A protein composed of two or more polypeptide chains Explanation of oligomeric protein
These notes were made for Biochem 3381 at the University of Western Ontario and cover secondary structure, quaternary structure, protein purification, and miscellaneous biochemistry techniques. Ramchandran plots and some secondary structure Quaternary Structure Misc Techniques Protein Purification Bonus! Code in R for generating Ramchandran plots like this one: Ramchandran plot phi |- c(value,value,value...) psi |- c(value,value,value...)…
The Hydrion QT-40 Quaternary Test Paper provides a simple, reliable and economical means to measure the concentration of quaternary sanitizers. Has a
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The Quaternary is conventionally subdivided into glacials and inter glacials, with further subdivision into stadials (shorter cold periods within interstadial
Temizleyici ve nemlendirici etkilerinden yararlanlmakta olan NeoStrata Bionic Face Serum 10 PHA / Bionik Serum kullanm ile beraber gece boyunca ok iyi bir nemlendirme salamaktadr. hii there thanks 4 the review. Does Collagen Have Quaternary Structure Remedy Cream Olivamine reduce wrinkles on hands It is completely safe and over the counter product. Eczema - an easy to understand guide covering causes diagnosis symptoms treatment and prevention plus additional Does Collagen Have Quaternary Structure Remedy Cream Olivamine in depth medical information. Optimals Optimals White Toner Oily Skin.. Botox is sold by the unit. Eczema herpes and psoriasis will begin to experience relief. Option 30 daclips.. SkinMedica Rejuvenative Toner. Time Delay Wrinkle Reduce Eye Cream Reviews dr mehran skin care products online; top wrinkle creams in canada; Time Delay Wrinkle how to use anti age serum Note the areas between the eyeows after Saratoga Springs area treatment with BOTOX. Theres a name for ...
We report the growth and characterization of quaternary AlGaInN. A combination of photoluminescence (PL), high-resolution x-ray diffraction (XRD), and Rutherford backscattering spectrometry (RBS) characterizations enables us to explore the contours of constant PL peak energy and lattice parameter as functions of the quaternary compositions. The observation of room temperature PL emission at 351nm (with 20% Al and 5% In) renders initial evidence that the quaternary could be used to provide confinement for GaInN (and possibly GaN). AlGaInN/GrdnN MQW heterostructures have been grown; both XRD and PL measurements suggest the possibility of incorporating this quaternary into optoelectronic devices. ...
Single crystals of Mo(1-x)Cr(x)AIB (quaternary representative of UBC) were synthesized by the high-temperature metal-solution method using aluminium flux, chromium, molybdenum metals and boron powder as starting materials. The mixture, with atomic ratio. ...
The technique of analytical ultracentrifugation (AUC) was developed by Svedberg and Lysholm in 1927 (1). With AUC one is able to determine molecular weight, shape and stoichiometry of macromolecules and macromolecular complexes.
ES domain oligomerization is necessary and sufficient for c18-induced motility. (A) Schematic of synthesis of ES domain monomer and dimer. Cleavage of an Fc-ES
Nicotinic acetylcholine, serotonin type 3, γ-amminobutyric acid type A, and glycine receptors are major players of human neuronal communication. They belong to the family of pentameric ligand-gated ion channels, sharing a highly conserved modular 3D structure. Recently, high-resolution structures of both open- and closed-pore conformations have been solved for a bacterial, an invertebrate, and a vertebrate receptor in this family. These data suggest that a common gating mechanism occurs, coupling neurotransmitter binding to pore opening, but they also pinpoint significant differences among subtypes. In this Review, we summarize the structural and functional data in light of these gating models and speculate about their mechanistic consequences on ion permeation, pathological mutations, as well as functional regulation by orthosteric and allosteric effectors.
TY - JOUR. T1 - Quaternary structure of LOV-domain containing polypeptide of Arabidopsis FKF1 protein. AU - Nakasako, Masayoshi. AU - Matsuoka, Daisuke. AU - Zikihara, Kazunori. AU - Tokutomi, Satoru. N1 - Funding Information: This work was supported by MEXT Japan to M.N. (No. 15076210) and S.T. (No. 13139205). The SAXS experiments were carried out as proposals to SPring-8 (Nos. 2003B-0141 and 2004A-0317).. PY - 2005/2/14. Y1 - 2005/2/14. N2 - Flavin-binding, Kelch repeat, F-box (FKF1) protein is a photoreceptor to regulate flowering of Arabidopsis. The protein has a light, oxygen and voltage (LOV)-sensing domain binding a flavin mononucleotide. The photo-activation of the domain is an indispensable step to initiate the cellular signaling for flowering. In the present study, a LOV-containing polypeptide of FKF1 was prepared by an overexpression system, and the quaternary structure of it was studied by size exclusion chromatography and small-angle X-ray scattering. The apparent molecular weight ...
GPIb-IX-V consists of four subunits : GPIbα (MW 135 kDa), GPIbβ (MW 26 kDa), GPIX (MW 20 kDa) and GPV (MW 82kDa). The complex is assembled such that GPIbα, GPIbβ and GPIX form a highly integrated protein complex in a 1:2:1 stoichiometry; and this associates weakly with GPV resulting in an overall stoichiometric ratio of 1:2:1:1 (Li and Emsley, 2013, Du et al., 1987, Luo et al., 2007, Mo et al., 2012) Each subunit of the complex is a type I transmembrane (TM) protein which consists of a leucine-rich repeat (LRR) ectodomain (extracellular domain), a single transmembrane helix, and a relatively short cytoplasmic tail (Li and Emsley, 2013, McEwan et al., 2011). The quaternary organisation of the receptor is facilitated by covalent and non-covalent interactions. The GPIbα subunit is linked to two GPIbβ subunits via membrane-proximal disulfide bonds (Figure 2), while GPIX associates itself tightly through non-covalent interactions with GPIb (Du et al., 1987, Luo et al., 2007, McEwan et al., ...
Two main results have emerged from this work. First, we have established that the quaternary organization of P2X subunits can be accurately defined using a combination of BRET and fluorescence complementation. Second, we have demonstrated that P2X5 and P2X2 subunits associate in a new heteromeric receptor with two stoichiometries. We have provided evidence that this receptor is endogenously expressed within specific neuronal populations, and displays functional properties that were previously thought to be unique to the P2X7 receptor (Surprenant et al., 1996).. Our cell surface assay (Chaumont et al., 2004) allowed a preliminary screening of P2X subunits interacting at the plasma membrane. Indeed, this approach has accurately identified subunits known to interact with P2X2 or P2X5, such as P2X3 and P2X1, respectively (Lewis et al., 1995; Haines et al., 1999; Lê et al., 1999; Surprenant et al., 2000), and revealed P2X2 subunits as a new assembly partner of P2X5. In native tissue, P2X2 and P2X5 ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
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2013.06.29 UPDATE: Heres a recording of my talk. Some more details: I received the A. Tovborg Jensen Award from the Royal Danish Academy of Sciences. Tovborg Jensen was a Danish chemist who brought crystallography, which he learned from Bragg himself, to Denmark. Upon his death he bequeathed a considerable sum of money to the Royal Danish Academy of Sciences to establish the award and associated lecture series names in honor of his colleagues Niels Bjerrum (he of the Bjerrum length), Johannes Brønsted (Brønsted acid/base theory) and Kaj Linderstrøm-Lang (who coined the terms primary, secondary, tertiary and quaternary protein structure ...
2013.06.29 UPDATE: Heres a recording of my talk. Some more details: I received the A. Tovborg Jensen Award from the Royal Danish Academy of Sciences. Tovborg Jensen was a Danish chemist who brought crystallography, which he learned from Bragg himself, to Denmark. Upon his death he bequeathed a considerable sum of money to the Royal Danish Academy of Sciences to establish the award and associated lecture series names in honor of his colleagues Niels Bjerrum (he of the Bjerrum length), Johannes Brønsted (Brønsted acid/base theory) and Kaj Linderstrøm-Lang (who coined the terms primary, secondary, tertiary and quaternary protein structure ...
As the Quaternary Period includes the present, any plant alive today has lived in the period, from lettuce to redwoods to seaweed. The Quaternary Period began roughly 2.5 million years ago and is...
Analytical ultracentrifugation (AUC) is a powerful technique for analyzing fundamental characteristics of macromolecules in solution, including size and shape, assembly state, and degree of p
Analytical Ultracentrifugation: (AUC) is a powerful method for characterizing solutions of macromolecules and is an indispensable tool for the quantitative
Purchase The Quaternary Period in the United States, Volume 1 - 1st Edition. Print Book & E-Book. ISBN 9780444514707, 9780080930473
Sometimes called bZIP motifs. A quaternary structure|dimer of two long alpha helix|alpha helices which look like forceps pinching a piece of DNA. These ...
Interleukin-2 (IL-2) is a small quaternary structure|monomeric protein 133 amino acid|amino acids in length. It is a very important cytokine in the immu...
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Gentaur molecular products has all kinds of products like :search , Gene Link \ 5_Fl Random Hexamer \ 26-4000-71 for more molecular products just contact us
Page contains details about DNA origami-AgNP trimer . It has composition images, properties, Characterization methods, synthesis, applications and reference articles :
Pentameric ligand-gated ion channels (pLGICs) mediate fast chemical signaling through global allosteric transitions. Despite the existence of several
Format: Monograph - paperback Size: 240 × 160 mm 156 pages ISBN: 9789461651938 Publication: May 13, 2016 Series: Acta Biomedica Lovaniensia 700 Languages: English ...
1GP9: A New Crystal Form of the Nk1 Splice Variant of Hgf/Sf Demonstrates Extensive Hinge Movement and Suggests that the Nk1 Dimer Originates by Domain Swapping
An Inter-subunit salt bridge is broken in the active conformation of AP2.Predicted location of the modified worm residues within the inactive (PBD ID: 2VGL) and
Tel: 029-853-5768, Fax: 029-853-6503. A New Way To Understand Quaternary Structure Changes of Hemoglobin upon Ligand Binding On the Basis of UV-Resonance Raman Evaluation of Intersubunit Interactions, S. Nagatomo, M. Nagai, and T. Kitagawa, J. Am. Chem. Soc., 133, 10101-10110 (2011 ...
Atomic models, 3B Scientific, Interactive Atomic Model According to Bohr, Class-Set, Interactive Atomic Model According to Bohr, Student-Set
The Vasp Tetramerization Domain is a Right-Handed Coiled Coil Based on a 15-Residue Repeat.. PubMed ID: 15-569-942. From NIHs 3D Print Exchange. ...
Pentameric ligand-gated ion channels (pLGICs) are extensively involved in fast synaptic transmission and play a key role in many different neurological processes, such as pain sensation, memory, and addiction. These receptors are known targets for a variety of established pharmacological agents with diverse clinical uses, but recent major progress in our understanding of pLGIC structure-function relationships allows for the enhanced discovery of new drugs with improved therapeutic potential and reduced adverse effects. This dissertation presents the integrated computational and experimental techniques employed towards this end for two different pLGICs, the α3 glycine receptor (GlyR) and the α7 nicotinic acetylcholine receptor (nAChR). Three primary accomplishments resulted from this work. First, an ensemble-based virtual screening protocol was developed to target the GlyR transmembrane domain (TMD). Small-scale screening calculations were performed as a pilot study and validated by functional ...
TY - JOUR. T1 - RESONANCE RAMAN SCATTERING STUDIES OF THE QUATERNARY STRUCTURE TRANSITION IN HEMOGLOBIN.. AU - Rousseau, D. L.. AU - Ondrias, M. R.. PY - 1983/1/1. Y1 - 1983/1/1. N2 - The oxygen-binding energy difference, the free energy of cooperativity, is a thermodynamic property, and its location can be determined from an examination of the deoxygenated and liganded proteins in both their high affinity and low affinity structures. An assessment of the energetic differences between these four steady-state protein structures should elucidate which interactions contain the free energy of cooperativity. Resonance Raman scattering plays a very important role in determining these interactions, since it is a very sensitive probe of the bonds involving the heme group. By examining the resonance Raman spectrum of the heme in both quaternary structures in the liganded and in the deoxy forms, it may in principle be determined if the free energy of cooperativity is localized in any heme-protein ...
TY - JOUR. T1 - Maintenance of the DNA-damage checkpoint requires DNA-damage-induced mediator protein oligomerization. AU - Usui, Takehiko AU - Foster, Steven. AU - Petrini, John H. J.. N1 - Open Archive. PY - 2009/1/30. Y1 - 2009/1/30. N2 - Oligomeric assembly of Brca1 C-terminal (BRCT) domain-containing mediator proteins occurs at sites of DNA damage. However, the functional significance and regulation of such assemblies are not well understood. In this study, we defined the molecular mechanism of DNA-damage-induced oligomerization of the S. cerevisiae BRCT protein Rad9. Our data suggest that Rad9s tandem BRCT domain mediates Rad9 oligomerization via its interaction with its own Mec1/Tel1-phosphorylated SQ/TQ cluster domain (SCD). Rad53 activation is unaffected by mutations that impair Rad9 oligomerization, but checkpoint maintenance is lost, indicating that oligomerization is required to sustain checkpoint signaling. Once activated, Rad53 phosphorylates the Rad9 BRCT domain, which attenuates ...
Septins are filament-forming proteins important for organizing the cortex of animal and fungal cells. In mammals, 13 septin paralogues were recently shown to assemble into core heterohexamer and heterooctamer complexes, which serve as building blocks for apolar filamentous structures that differ among cell types. To determine how tissue-specific septin paralogue expression may shape core heteromer repertoires and thereby modulate properties of septin filaments, we devised protocols to analyze native septin heteromers with distinct numbers of subunits. Our evidence based on genetically manipulated human cells supports and extends recent concepts of homology subgroup-restricted assembly into distinct categories of apolar heterohexamers and heterooctamers. We also identify a category of tetramers that have a subunit composition equivalent to an octameric building block. These atypical tetramers are prevalent in lymphocytes and neural tissues, in which octamers are abundant but hexamers are rare. ...
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CIMmultus™ stands for: Convective mass transfer, reduced backpressure, and minimal sample clogging Fast product isolation and concentration of diluted
CIMmultus™ stands for: Convective mass transfer, reduced backpressure, and minimal sample clogging Fast product isolation and concentration of diluted 6 (RE = Eu-Yb, Y) have been converted from their colloidal precursor spheres (amor-phous phase form) synthesized via homogeneous pre-cipitation [16]. In this work, micron-sized moydite spheres of M(B(OH) 4)CO 3 (M = Y, Tb, Eu, Bi) quaternary system have been rapid synthesized by microwave pro-cessing, and the precursor converted into (Y, Tb, Eu ... ...
"Crystal structure of peanut lectin, a protein with an unusual quaternary structure". Proceedings of the National Academy of ... "Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its ... The work on lectins demonstrated the need for considering open quaternary structures when dealing with multimeric proteins and ... His main area of research is protein structures. His contributions have been towards the structure and carbohydrate specificity ...
"The emergence of protein complexes: Quaternary structure, dynamics and allostery. Colworth Medal Lecture". Biochemical Society ... Collinson, I (2005). "The structure of the bacterial protein translocation complex SecYEG". Biochemical Society Transactions. ... Structural studies of reversible protein phosphorylation and protein phosphatases". Biochemical Society Transactions. 27 (6): ... Rouse, J (2009). "Control of genome stability by SLX protein complexes". Biochemical Society Transactions. 37 (Pt 3): 495-510. ...
"The emergence of protein complexes: quaternary structure, dynamics and allostery". Biochemical Society Transactions. 40 (3): ... seeks to elucidate the principles of protein structure evolution, higher order protein structure and protein folding, and the ... Han, Jay (2007). Structure, function and evolution of protein-protein interactions (PhD thesis). University of Cambridge. ... A fundamental discovery was her work to define key biophysical mechanisms in protein complex assembly, showing that protein ...
As a whole, this is called a protein's quaternary structure. The quaternary structure is generated by the formation of ... Single tertiary protein structures can also assemble to form protein complexes composed of multiple independently folded ... Between 5 and 1000 milliseconds after protein folding initiation, three-dimensional structures of proteins, known as secondary ... The folding of most proteins from a primary (linear) sequence of amino acids to a three-dimensional structure is governed by ...
"Signature of quaternary structure in the sequences of legume lectins". Protein Eng. 14 (10): 735-45. doi:10.1093/protein/14.10. ... Despite the conserved structure of the legume lectin subunit, they can adopt a wide range of quaternary structures. The reason ... "The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked ... The legume lectins are also interesting from the point of view of protein structure. ...
This receptor is a protein with an (αβ)2 quaternary structure. The two large α-subunits are extracellular, while the smaller β- ... The phosphoacceptors often reside within loops in the protein structure suitably termed 'activation loops'. The structures of ... "Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: structure of ... Petsko, GA and Ringe, D 2009, 'Protein Structure and Function', Oxford University Press Inc., New York, U.S.A Summers KC, Shen ...
Quaternary structure Protein complex Macromolecular assembly Biomolecular complex Neuman, Nicole (2016). "The Complex ...
"AU-rich RNA-binding induces changes in the quaternary structure of AUH". Proteins. 75 (2): 360-72. doi:10.1002/prot.22246. PMID ... "Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase". Structure. 9 (12): 1253- ... "A bifunctional protein regulates mitochondrial protein synthesis". Nucleic Acids Research. 42 (9): 5483-94. doi:10.1093/nar/ ... "Entrez Gene: AU RNA binding protein/enoyl-CoA hydratase". Mercimek-Mahmutoglu S, Tucker T, Casey B (Nov 2011). "Phenotypic ...
An Effective Method for Characterization of Protein Quaternary Structure". Analytical Chemistry. 91 (1): 190-191. doi:10.1021/ ... and the degree of unfolding for protein structure. Analysis of protein structure unfolding is the most commonly used ... To quantify proteins, peptides are labeled with chemical tags that have the same structure and nominal mass, but vary in the ... The unique dissociation patterns help discover the Quaternary structure of the complex. The symmetric charge distribution and ...
... a protein with an unusual quaternary structure". Proceedings of the National Academy of Sciences of the United States of ... He discovered the unusual quaternary structure of peanut agglutinin and a novel lectin fold in Jacalin as well as the ... protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex". ... He popularized Protein A as a tool in immunology. He discovered the broad substrate specificity of a key enzyme of biotin ...
... has a quaternary structure characteristic of many multi-subunit globular proteins. Most of the amino acids in ... Each subunit is composed of a protein chain tightly associated with a non-protein prosthetic heme group. Each protein chain ... Hemoglobin's quaternary structure comes from its four subunits in roughly a tetrahedral arrangement. In most vertebrates, the ... In all proteins, it is the amino acid sequence that determines the protein's chemical properties and function. There is more ...
"Protein super-secondary structure and quaternary structure topology: theoretical description and application". Current Opinion ... The progress in 3D structure determination of membrane proteins by X-ray crystallography and cryo electron microscopy has ... They also develops algorithms to solve problems in molecular biology, ranging from atomic protein structure analysis to ... and RNA-protein complexes. Important structures of macromolecular complexes were determined in CEF. Examples for important ...
Barker S, Mayo KH (January 1995). "Quarternary structure amplification of protein folding differences observed in 'native' ... The gene for human PF4 is located on human chromosome 4. Platelet factor-4 is a 70-amino acid protein that is released from the ... Walz DA, Wu VY, de Lamo R, Dene H, McCoy LE (December 1977). "Primary structure of human platelet factor 4". Thrombosis ... Zhang X, Chen L, Bancroft DP, Lai CK, Maione TE (July 1994). "Crystal structure of recombinant human platelet factor 4". ...
Bertoni M, Kiefer F, Biasini M, Bordoli L, Schwede T (September 2017). "Modeling protein quaternary structure of homo- and ... Between the AbrB superfamily protein structure and the SymE protein structure, there are several key hydrophobic residues that ... Guex N, Peitsch MC, Schwede T (June 2009). "Automated comparative protein structure modeling with SWISS-MODEL and Swiss- ... July 2018). "SWISS-MODEL: homology modelling of protein structures and complexes". Nucleic Acids Research. 46 (W1): W296-W303. ...
The apoptosome is a large quaternary protein structure formed in the process of apoptosis. Its formation is triggered by the ... "Structure of the Drosophila Apoptosome at 6.9 Å Resolution." Structure. 2011 January;19(1):128-140. S. Qi; Y. Pang; Q. Hu; Q. ... "Structure of an apoptosome-procaspase-9 CARD complex." Structure. 2010 May;18(5):571-83. Acehan D, Jiang X, Morgan DG, Heuser ... WD-40 repeats are sequences around 40 amino acids long which end in Trp-Asp and are typically involved in protein-protein ...
AnPRT has four domains and its quaternary structure consists of two identical protein structures. Each domain of AnPRT contains ... The secondary structure of AnPRT consists mainly of alpha helices with a beta sheet within each domain. There are homologues of ... All of these organisms are alike in the sense that they make all of the amino acids needed for proper protein formation (also ... 12 structures have been solved for this class of enzymes, with PDB accession codes 1GXB, 1KGZ, 1KHD, 1O17, 1V8G, 1VQU, 1ZVW, ...
Proteins contain 4 elements in regards to their structure: primary, secondary, tertiary and quaternary. The linear amino acid ... The quaternary structure refers to the way multiple chains of polypeptides fold together. Proteins have many different ... Proteins such as actin, microtubules and intermediate filaments provide structure to the cell. Another class of proteins are ... Membrane proteins can be associated with the plasma membrane in different ways, depending on their structure. These proteins ...
Quaternary structure: the structure formed by several protein molecules (polypeptide chains), usually called protein subunits ... Structure determination. Discovering the tertiary structure of a protein, or the quaternary structure of its complexes, can ... Protein structure prediction. Most proteins fold into unique 3-dimensional structures. The shape into which a protein naturally ... Structure. The crystal structure of the chaperonin, a huge protein complex. A single protein subunit is highlighted. ...
Tang, L.; Stith, L; Jaffe, EK (2005). "Substrate-induced Interconversion of Protein Quaternary Structure Isoforms". Journal of ... "Simultaneous optimization of enzyme activity and quaternary structure by directed evolution". Protein Science. 14 (8): 2103-14 ... 2001). "X-ray structure of HPr kinase: A bacterial protein kinase with a P-loop nucleotide-binding domain". The EMBO Journal. ... Tong, E. K.; Duckworth, Harry W. (1975). "Quaternary structure of citrate synthase from Escherichia coli K 12". Biochemistry. ...
It is also useful for determining the tertiary structure and quaternary structure of purified proteins. SEC is used primarily ... This technique is used for mild separation and recovery of proteins and protection of their biological activity in protein ... For example, a protein which is only slightly smaller than a pore might enter the pore but does not easily leave once inside. ... The interaction strength depends not only on the functional groups present in the structure of the analyte molecule, but also ...
This results in the formation of a quaternary structure that is characteristic of this protein. This TRFH domain also allows ... There are 4 domain categories on the TERF2 protein that allow it to bind to both other proteins in the shelterin protein ... De Lange isolated the new Myb-containing protein sequence and called it TERF2. TERF2 has a similar structure to that of TERF1. ... TERF2 is also known to recruit certain client proteins, also known as accessory factors. These client proteins are often ...
... modelling protein tertiary and quaternary structure using evolutionary information". Nucleic Acids Research. 42 (W1): 195-201. ... SWISS-MODEL Homology modelling Protein structure prediction Protein structure prediction software CASP (Critical Assessment of ... modelling methods make use of experimental protein structures ("templates") to build models for evolutionary related proteins ... SWISS-MODEL pipeline comprises the four main steps that are involved in building a homology model of a given protein structure ...
... homology modeling of protein tertiary structures and quaternary structures; validating protein structures, notably those ... Hooft, RW; Vriend, G; Sander, C; Abola, EE (23 May 1996). "Errors in protein structures". Nature. 381 (6580): 272. doi:10.1038/ ... correcting protein structures; visualising macromolecules and their interaction partners (for example, lipids, drugs, ions, and ... WHAT IF is a computer program used in a wide variety of computational (in silico) macromolecular structure research fields. The ...
Proteins have tertiary and quaternary structures that can be degraded or cause aggregation at room temperature. This can impact ... In protein formulations, stabilizers are added to replace the water and preserve the structure of the molecule. Before ... In dealing with protein pre-formulation, the important aspect is to understand the solution behavior of a given protein under a ... Practical approaches to protein formulation development. in "Rationale Design of stable protein formulations-theory and ...
Hanemaaijer R, Westphal AH, Van Der Heiden T, De Kok A, Veeger C (Feb 1989). "The quaternary structure of the dihydrolipoyl ... Protein Structure and Molecular Enzymology. 1385 (2): 353-66. doi:10.1016/S0167-4838(98)00079-X. PMID 9655933. ... The cubic core structure, found in species such as Azotobacter vinelandii, is made up of 24 subunits total. The catalytic ... These structure then form the catalytic core of the pyruvate dehydrogenase complex which not only catalyzes the reaction that ...
There is no evidence to suggest that FAM76A interacts with other proteins to form a quaternary structure. The protein ... "Phyre2".[permanent dead link] "I-TASSER Protein Structure & Function Predictions". "PSORT II Prediction". "NCBI Geo Profile". " ... The amino acid composition of FAM76A protein showed amino acid frequencies within 1.5% of that of normal human proteins for all ... FAM76A is a protein that in Homo sapiens is encoded by the FAM76A gene. Notable structural characteristics of FAM76A include an ...
Hutcheson (1997) found that the tertiary and quaternary structures of protein elicitors are dependent on elicitor activity. ... RLKs are transmembrane proteins that consists of inner, outer, and central membrane regions. Being proteins, they also have an ... In this domain, phosphorylation catalyzes a protein kinase cascade leading to a response. In FLS2, this response elicits ... The transmembrane domain is where proteins transition from extracellular to intracellular. This region is usually very ...
... has a quaternary structure characteristic of many multi-subunit globular proteins.[34] Most of the amino acids in ... Each subunit is composed of a protein chain tightly associated with a non-protein prosthetic heme group. Each protein chain ... Structure of human haemoglobin. α and β subunits are in red and blue, and the iron-containing heme groups in green. From PDB: ... In all proteins, it is the amino acid sequence that determines the protein's chemical properties and function. ...
... and quaternary structures of proteins and nucleic acids. It also plays an important role in the structure of polymers, both ... Ege, Seyhan (2003) Organic Chemistry: Structure and Reactivity. Houghton Mifflin College. ISBN 0618318097. pp. 30-33, 67. " ...
Structure of the octahedral n-butyllithium hexamer, (C4H9Li)6.[138] The aggregates are held together by delocalised covalent ... In particular, the quaternary ammonium cations (NR+. 4) are very useful since they are permanently charged, and they are often ... The balance between potassium and sodium is maintained by ion transporter proteins in the cell membrane.[231] The cell membrane ... Structure and Bonding. 21: 89-144. doi:10.1007/BFb0116498. ISBN 978-3-540-07109-9. . Retrieved 4 October 2013.. ...
A reduction in these linkages has the potential to change the tertiary structure, causing the protein to unfold. This ... quaternary ammonium compounds and detergents have little effect on endospores. However, sterilant alkylating agents such as ... after further studies this group concluded that the structure of the spore coat protein was different from keratin.[10] When ... Small acid-soluble proteins (SASPs) are found in endospores. These proteins tightly bind and condense the DNA, and are in part ...
... results in small changes in tertiary structure at the subunit interface leading to large changes in quaternary structure.[8] ... Structure[edit]. The glycogen phosphorylase monomer is a large protein, composed of 842 amino acids with a mass of 97.434 kDa ... Residues 397-437 form this structure, which allows the protein to covalently bind to the glycogen chain a full 30 Å from the ... I. Isolation and characterization of the protein-glycogen complex". Journal of Biological Chemistry. 245 (24): 6642-6648. PMID ...
... which is one of the primary influences on the three-dimensional structures of proteins.[18] ... These species are not amines but are quaternary ammonium cations and have a charged nitrogen center. Quaternary ammonium salts ... StructureEdit. Alkyl aminesEdit. Alkyl amines characteristically feature tetrahedral nitrogen centers. C-N-C and C-N-H angles ... 3) are the most common positively charged moieties in proteins, specifically in the amino acid lysine.[16] The anionic polymer ...
... by comparing sequences of DNA or proteins. The result of a successful analysis is a hierarchy of clades - groups that share a ... cells with complex internal structures, may have been present earlier, their evolution speeded up when they acquired the ... Although this early study compared proteins from apes and humans, most molecular phylogenetics research is now based on ... "Some problematic shallow-marine structures". Marine Geol. 4 (3): 227-232. Bibcode:1966MGeol...4..227M. doi:10.1016/0025-3227( ...
Structure of the influenza virion. The hemagglutinin (HA) and neuraminidase (NA) proteins are shown on the surface of the ... while quaternary ammonium compounds can be used with alcohol so that the sanitizing effect lasts for longer.[134] In hospitals ... matrix 1 protein), M2, NS1 (non-structural protein 1), NS2 (other name is NEP, nuclear export protein), PA, PB1 (polymerase ... Structure, properties, and subtype nomenclature. Influenzaviruses A, B, C, and D are very similar in overall structure.[7][59][ ...
... such as stabilizing forces in their tertiary and quaternary structures which prevent degradation during digestion. Many ... The harmful proteins are those that do not break down due to the strong bonds of the protein. IgE antibodies bind to a receptor ... Many food allergies are caused by hypersensitivities to particular proteins in different foods. Proteins have unique properties ... Are the transferred proteins resistant to digestion - a trait shared by many allergenic proteins?[115] Genes approved for ...
J. Elks (14 November 2014). The Dictionary of Drugs: Chemical Data: Chemical Data, Structures and Bibliographies. Springer. pp ... Protein binding. ~92%[1]. Metabolism. Hepatic (CYP3A4/5) and intestinal (first-pass)[1][4]. ...
"Protein Spotlight (29). Retrieved 14 September 2006.. *^ Weimann, Anya (4 July 2007) Evolution of platypus venom revealed. ... The oldest discovered fossil of the modern platypus dates back to about 100,000 years ago, during the Quaternary period. The ... "Bone Inner Structure Suggests Increasing Aquatic Adaptations in Desmostylia (Mammalia, Afrotheria)". PLoS ONE. 8 (4): e59146. ... composed largely of defensin-like proteins (DLPs), three of which are unique to the platypus.[30] The DLPs are produced by the ...
Quaternary structure: the structure formed by several protein molecules (polypeptide chains), usually called protein subunits ... Structure determination. Discovering the tertiary structure of a protein, or the quaternary structure of its complexes, can ... Protein structure prediction. Most proteins fold into unique 3-dimensional structures. The shape into which a protein naturally ... Structure. The crystal structure of the chaperonin, a huge protein complex. A single protein subunit is highlighted. ...
Some migratory birds have adapted to use protein from many parts of their bodies, including protein from the intestines, as ... Maina, John N. (November 2006). "Development, structure, and function of a novel respiratory organ, the lung-air sac system of ... See also: Late Quaternary prehistoric birds, List of extinct birds, and Raptor conservation ... Domesticated birds raised for meat and eggs, called poultry, are the largest source of animal protein eaten by humans; in 2003 ...
The original synapsid skull structure has one hole behind each eye, in a fairly low position on the skull (lower right in this ... "Assessing the Cretaceous superordinal divergence times within birds and placental mammals by using whole mitochondrial protein ... There is little correspondence between the structure of the family (what was descended from what) and the dates of the earliest ... Modern mammals have respiratory turbinates, convoluted structures of thin bone in the nasal cavity. These are lined with mucous ...
See also: Protein structure. *In quaternary structure denaturation, protein sub-units are dissociated and/or the spatial ... Denaturation is a process in which proteins or nucleic acids lose the quaternary structure, tertiary structure, and secondary ... 3) Tertiary Structure : three-dimensional structure of alpha helixes and beta helixes folded 4) Quaternary Structure : three- ... Functional protein showing a quaternary structure 2) when heat is applied it alters the intramolecular bonds of the protein 3) ...
The structure of a flower can also be expressed by the means of floral diagrams. The use of schematic diagrams can replace long ... Whereas the pollen of animal-pollinated flowers tends to be large-grained, sticky, and rich in protein (another "reward" for ... A flower, sometimes known as a bloom or blossom, is the reproductive structure found in flowering plants (plants of the ... Structure. Although the arrangement described above is considered "typical", plant species show a wide variation in floral ...
Densmore III, L. D. & Dessauer, H. C. (1984). "Low levels of protein divergence detected between Gavialis and Tomistoma: ... During the Quaternary, Gavialis dispersed as far as Java via the Siva-Malayan route, which did not require saltwater crossings ... it was suggested that the gharial and all the other crocodilians form a sister group as the structure of its tail muscles is ... Others suggested that it evolved much later than other crocodilians because of its low levels of blood proteins. As it shares ...
"Osteological Correlates of Cephalic Skin Structures in Amniota: Documenting the Evolution of Display and Feeding Structures ... the same type of protein that makes up hair and fingernails.[5] Both African species and the Sumatran rhinoceros have two horns ... "Evolution and extinction of the giant rhinoceros Elasmotherium sibiricum sheds light on late Quaternary megafaunal extinctions ... protective skin formed from layers of collagen positioned in a lattice structure. They generally eat leafy material, although ...
Eaten for about a month, the pap provides a supplementary source of protein at a transition time from a milk to a leaf diet.[88 ... "Quaternary Science Reviews. 27 (27-28): 2516-21. doi:10.1016/j.quascirev.2008.08.026.. ... "Genetic variation and structuring in the threatened koala populations of Southeast Queensland". Conservation Genetics. 11 (6): ... 2 cause Eucalyptus trees to reduce protein and increase tannin concentrations in their leaves, reducing the quality of the food ...
Protein structure determination from sparse experimental data - an introductory presentation. *Protein NMR Protein NMR ... Structure calculation[edit]. Nuclear magnetic resonance structure determination generates an ensemble of structures. The ... However, the X-ray diffraction structure may not exist, and, since the proteins in solution are flexible molecules, a protein ... See also: Protein dynamics. In addition to structures, nuclear magnetic resonance can yield information on the dynamics of ...
Template:DNA and protein biosynthesis navs(edit talk links history)- Genetics ({{Protein biosynthesis navs}}, R) ... Proteins *domains. *Structure *primary. *secondary. *tertiary. *quaternary. Disease. *Replication and repair. *Transcription ...
... proteins are classically treated with SDS to denature the native tertiary and quaternary structures, allowing the separation of ... This process maintains a matrix of proteins that preserves the structure of the organ and often the microvascular network. The ... Structure of surfactant phases in water[edit]. In the bulk aqueous phase, surfactants form aggregates, such as micelles, where ... Composition and structure[edit]. Surfactants are usually organic compounds that are amphiphilic, meaning they contain both ...
... a round stone structure. Related stone structures called Tupa look very similar to the hare oka, except that the Tupa were ... Midden contents show that the main source of protein was tuna and dolphin. With the loss of the trees, there was a sudden drop ... Flenley, J. R.; King, Sarah M. (1984). "Late Quaternary pollen records from Easter Island". Nature. 307 (5946): 47. Bibcode: ... By the 18th century, silanders were largely sustained by farming, with domestic chickens as the primary source of protein.[29] ...
... a round stone structure. Related stone structures called Tupa look very similar to the hare oka, except that the Tupa were ... Midden contents show that the main source of protein was tuna and dolphin. With the loss of the trees, there was a sudden drop ... Flenley, J. R.; King, Sarah M. (1984). "Late Quaternary pollen records from Easter Island". Nature. 307 (5946): 47. Bibcode: ... In this context ahu referred to a small structure sometimes covered with a thatched roof where sacred objects, including ...
Structure and reactivity[edit]. Muscarine mimics the function of the natural neurotransmitter acetylcholine in the muscarinic ... M1, M3 and M5 interact with Gq proteins to stimulate phosphoinositide hydrolysis and the release of intracellular calcium. M2 ... Being a quaternary ammonium salt, muscarine is less completely absorbed from the gastrointestinal tract than tertiary amines, ... Final proof of the structure was given by Franz Jellinek and colleagues in 1957 with the help of X-ray diffraction analysis;[4] ...
a quaternary combinator in combinatory logic. *. ψ. {\displaystyle \psi }. represents: *the wave function in the Schrödinger ... the tau in biochemistry, a protein associated to microtubules. *the golden ratio 1.618... (although φ (phi) is more common) ... the fine structure constant in physics. *the angle of attack of an aircraft ...
In such proteins, the pigments are arranged to work together. Such a combination of proteins is also called a light-harvesting ... The oxidation of water is catalyzed in photosystem II by a redox-active structure that contains four manganese ions and a ... In plants, these proteins are held inside organelles called chloroplasts, which are most abundant in leaf cells, while in ... To combat this problem, a series of proteins with different pigments surround the reaction center. This unit is called a ...
Interactive image of nucleic acid structure (primary, secondary, tertiary, and quaternary) using DNA helices and examples from ... In bioinformatics, a sequence alignment is a way of arranging the sequences of DNA, RNA, or protein to identify regions of ... Nucleic acids also have a secondary structure and tertiary structure. Primary structure is sometimes mistakenly referred to as ... Frequently the primary structure encodes motifs that are of functional importance. Some examples of sequence motifs are: the C/ ...
Structure[edit]. The complete quaternary structure of Fel d 1 has been determined.[1] The allergen is a tetrameric glycoprotein ... Fel d 1 is a protein that in cats is encoded by the CH1 (chain 1/Fel d 1-A) and CH2 (chain 2/Fel d 1-B) genes.[2][3] ... Crystallographic structure of the Fel d 1 dimer, the primary allergen present in cat saliva.[1] ... Griffith IJ, Craig S, Pollock J, Yu XB, Morgenstern JP, Rogers BL (April 1992). "Expression and genomic structure of the genes ...
"Disease-causing Mutations and protein structure". UCL Biochemistry BSM Group. Retrieved 2007-04-02.. [permanent dead link] ...
... protein-protein interaction when discussing quaternary structure of proteins and consider all assemblies of proteins as protein ... "Predicting protein quaternary structure by pseudo amino acid composition". Proteins: Structure, Function, and Bioinformatics. ... Protein quaternary structure can be determined using a variety of experimental techniques that require a sample of protein in a ... Protein quaternary structure is the number and arrangement of multiple folded protein subunits in a multi-subunit complex. It ...
SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information.. Biasini M1, Bienert S1, ... SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 2014 Jul 1; ... SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 2014 Jul 1; ... Protein structure homology modelling has become a routine technique to generate 3D models for proteins when experimental ...
Generate Quaternary structure of protein from monomer *Next message (by thread): [BiO BB] Generate Quaternary structure of ... Generate Quaternary structure of protein from monomer *Next message (by thread): [BiO BB] Generate Quaternary structure of ... Reply to James Strond answer , , Yes, for template structure has a quaternary structure , and therefore are known. , , My Query ... BiO BB] Generate Quaternary structure of protein from monomer. Dr.Nagasuma Chandra nchandra at Fri Mar 4 ...
The three resulting {open_quotes}snapshots{close_quotes} of possible structures show that their variable-domain interactions ... Tryptophan residues are commonly found in interfaces between proteins and their subunits, and histidines have been implicated ... the observed solvent response are tryptophans and histidines located between the two variable domains in the dimeric structure ... the structure of multi-subunit protein (immunoglobulin light chain) was solved in three crystal forms, differing only in the pH ...
... Chi-Hua Tung,1 Chi-Wei Chen, ... A Prediction System for Protein Quaternary Structure Attributes Using Block Composition," BioMed Research International, vol. ...
K.-C. Chou and Y.-D. Cai, "Predicting protein quaternary structure by pseudo amino acid composition," Proteins: Structure, ... H. Sund and K. Weber, "The quaternary structure of proteins," Angewandte Chemie International Edition in English, vol. 5, no. 2 ... QuaBingo: A Prediction System for Protein Quaternary Structure Attributes Using Block Composition. Chi-Hua Tung,1 Chi-Wei Chen, ... S.-W. Zhang, Q. Pan, H.-C. Zhang, Y.-L. Zhang, and H.-Y. Wang, "Classification of protein quaternary structure with support ...
The protein quaternary structure of the complex is divided into five categories, namely, monomer, dimer, trimer, tetramer, and ... The classification of the protein quaternary structure complex for the post-genome era of proteomics research will be of great ... Classification systems among protein quaternary structures have not been widely developed. Therefore, we designed the ... The dimer structure of transcription factors is involved in gene regulation, but the trimer structure of virus-infection- ...
"Protein Structure, Quaternary" by people in this website by year, and whether "Protein Structure, Quaternary" was a major or ... "Protein Structure, Quaternary" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... Protein Structure, Quaternary*Protein Structure, Quaternary. *Protein Structures, Quaternary. *Quaternary Protein Structures ... Below are the most recent publications written about "Protein Structure, Quaternary" by people in Profiles. ...
Compared to our knowledge of protein secondary and tertiary structure, the driving forces behind protein quaternary structure ... On the Quaternary Structure of Macromolecular Protein Complexes in the Absence of Bulk Solvent. Add to your list(s) Download to ... In this presentation, the gas-phase quaternary structures and structural transitions of protein assemblies that cover a range ... On the Quaternary Structure of Macromolecular Protein Complexes in the Absence of Bulk Solvent ...
Cofactor Interactions for a Helical Transmembrane Protein Complex through 1H Spin Diffusion with MAS NMR Spectroscopy ... Helical Transmembrane Protein Complex 1 H Spin Diffusion magic angle Quaternary Structure helical transmembrane model protein ... and Quaternary Structure along with Protein−Cofactor Interactions for a Helical Transmembrane Protein Complex through ,sup,1,/ ... Probing secondary, tertiary, and quaternary structure along with protein−cofactor interactions through ,sup,1,/sup,H spin ...
... quaternary structure, and intracellular transport of vesicular stomatitis virus G protein. R W Doms , R W Doms ... quaternary structure, and intracellular transport of vesicular stomatitis virus G protein.. J Cell Biol 1 July 1988; 107 (1): ... The vesicular stomatitis virus glycoprotein (G protein) is an integral membrane protein which assembles into noncovalently ... These mutant proteins, whose ectodomains were identical to the wild-type by several assays, were either transported to the cell ...
protein structure, quaternary; Quaternary Protein Structure. The quaternary structure of the protein is the association of ... A dodecameric protein has a quaternary structure consisting of 12 protein subunits in a complex. Protein Structure, Quaternary ... For teaching basic protein structure, tertiary structure are involved in stabilizing quaternary structure quaternary structure ... and quaternary. Quaternary Protein - Structure The quaternary protein structure involves the clustering of several individual ...
Protein Proteins are compounds composed of carbon, hydrogen, oxygen , and nitrogen , which are arranged as strands of amino ... Quaternary structure: The highest level of structure found in proteins.. Secondary structure: Certain highly regular three- ... Protein Structure , Skip to main content Protein structure Proteins are chains of amino acids that fold into a three- ... Protein Structure. The order of the amino acids in a protein dictates the primary structure of the protein. While other levels ...
... natively unstructured proteins) and exist in random conformations. The function of proteins depends on their structure,… ... and they show the greatest variety of structures. Many have intricate three-dimensional folding patterns that result in a ... Proteins are the largest and most varied class of biological molecules, ... Quaternary Structure. Some proteins are composed of more than one polypeptide chain. In such proteins, quaternary structure ...
Collagen Protein Structure Quaternary For Cream 30s. You want to reduce lines and wrinkles Is there a recovery period after ... Collagen Protein Structure Quaternary For Cream 30s mostly used as an outer packaging in combination with our ultra clean ... Introduction Preparations of botulinum Collagen Protein Structure Quaternary For Cream 30s toxin (BoNT-A) have rapidly become ... Unlike creams and serums which act from the outside you Banish dark circles under your Collagen Protein Structure Quaternary ...
Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These ... Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its ... This quaternary structure with a unique dimeric interface lends the oligomeric protein greater stability, which may be of ... Crystal structure of the single-stranded dna-binding protein from mycobacterium tuberculosis. *DOI: 10.2210/pdb1UE7/pdb ...
From primary to quaternary structure. The primary structure of a protein, i.e., its amino acid sequence, contains all the ... The protein sequence determines the native fold of a protein, and protein structure determines the function of a protein, be ... Even when the structure of a protein has not been determined, 3D-structures may be available for related proteins, serving as ... Protein 3D-structures help to classify proteins, assign proteins with low sequence similarity to known families, or identify ...
Automatic inference of protein quaternary structure from crystals. Ponstingl, H, Kabir, T and Thornton, JM ... Coclustering the C. elegans and C. briggsae proteins reveals 2,169 protein families of two or more members. Most of these are ... The unfolded protein response is partially activated in PEL, but is fully activated in plasma cell tumors, linking endoplasmic ... Motivation: Structured non-coding RNAs (ncRNAs) have a very important functional role in the cell. No distinctive general ...
42a-2 FIBROUS PROTEINS…: QUATERNARY STRUCTURE 4º 1bbb.pdb-500 ... Not all proteins have quaternary structures (e.g. lysozymes and ... QUATERNARY STRUCTURE. 4º. * FIBROUS PROTEINS: STRUCTURAL ROLE. COLLAGEN: a structural protein, the most abundant fibrous ... QUATERNARY STRUCTURE 4º 1bbb.pdb-500 (figure_02_42a-2 FIBROUS PROTEINS…. ... GLOBULAR PROTEINS: METABOLIC ROLE. HAEMOGLOBIN : a transport protein which involves the transport of oxygen in blood; found in ...
What Are Proteins? Primary, Secondary, Tertiary, and Quaternary Structure. 2 years ago ... How does primary structure influence tertiary structure? What is the secondary structure of a protein? What is tertiary for ... What Are Proteins? Making and Breaking Proteins. 6 years ago. How are proteins made? What is the difference between ... What Are Proteins? Central Dogma of Molecular Biology. 6 years ago. First part of a series looking at proteins. This hub ...
Receptor Quaternary Organization Explains G Protein-Coupled Receptor Family Structure Felce JH., Latty SL., Knox RG., Mattick ... Protein clue to sudden cardiac death * Alzheimers Research UK Oxford Drug Discovery Institute to fast-track new dementia ... Raised blood pressure and diabetes alter brain structure to slow thinking speed and memory ...
Quaternary structure of LOV-domain containing polypeptide of Arabidopsis FKF1 protein. In: FEBS Letters. 2005 ; Vol. 579, No. 5 ... Quaternary structure of LOV-domain containing polypeptide of Arabidopsis FKF1 protein. Masayoshi Nakasako, Daisuke Matsuoka, ... Quaternary structure of LOV-domain containing polypeptide of Arabidopsis FKF1 protein. / Nakasako, Masayoshi; Matsuoka, Daisuke ... keywords = "FKF1 protein, LOV domain, Photoperiodism, Quaternary structure, Small-angle X-ray scattering", ...
T-to-T(High) Quaternary Transitions in Human Hemoglobin: alphaN97A deoxy low-salt. ... Structure Factors. EDS map. EDS difference map. Assembly composition XML. Assembly 1 (mmCIF; gz). Assembly 1 (atom only; mmCIF) ... quaternary transitions. Kavanaugh JS, Rogers PH, Arnone A ... Structure domain: * Occurring in:. *Hemoglobin subunit alpha. * ...
Automated evaluation of quaternary structures from protein crystals journal, April 2018 * Bliven, Spencer; Lafita, Aleix; ... LGA: a method for finding 3D similarities in protein structures journal, July 2003 * Zemla, A. ... Crystal Structure of an Unusual Single-Stranded DNA-Binding Protein Encoded by Staphylococcal Cassette Chromosome Elements ... Proteins. Additional Journal Information: Journal Name: Proteins; Journal ID: ISSN 0887-3585. Publisher: Wiley. Country of ...
Breaking Apart the Quaternary Structure[edit]. The quaternary structure of a protein can be denatured by breaking the covalent ... Tertiary Structure[edit]. The tertiary structure of a protein is the three-dimensional structure of the protein. This three- ... Human attempt to manipulate protein assemblies (Quaternary Structures)[edit]. Controlling the quaternary structures is ... Naming Quaternary Structures[edit]. In naming quaternary structures, the number of subunits (tertiary structure) and the suffix ...
Quaternary structure: the structure formed by several protein molecules (polypeptide chains), usually called protein subunits ... Structure determination. Discovering the tertiary structure of a protein, or the quaternary structure of its complexes, can ... Protein structure prediction. Most proteins fold into unique 3-dimensional structures. The shape into which a protein naturally ... Structure. The crystal structure of the chaperonin, a huge protein complex. A single protein subunit is highlighted. ...
Learn about the conformation levels of protein and polypeptide structure. ... There are four levels of structure found in polypeptides and proteins. ... Quaternary Structure. Quaternary structure is used to describe proteins composed of multiple subunits (multiple polypeptide ... The most common example used to illustrate quaternary structure is the hemoglobin protein. Hemoglobins quaternary structure is ...
Primary Structure , Secondary Structure , Tertiary Structure , Quaternary Structure , Hydrophobic Collapse , Levinthals ... Definitions of the important terms you need to know about in order to understand Amino Acids and Proteins, including Amino Acid ... Quaternary Structure The fourth level of protein structure that refers to the spatial arrangement of the subunits within the ... Secondary Structure The second level of protein structure where the linear sequence of proteins begins to fold into regular ...
Probable Quaternary Structures: specific oligomers: 1k28, 1k93, virus capsids. vs. Crystal Contacts (4mdh). *ConSurf: regions ... Protein 3D Structure & Bioinformatics: Visualization & Analysis in Protein Explorer Graduate School of Frontier Biosciences, ... Searching by structure without reference to sequence: (Try the bacterial cell division protein 1FSZ§.) Structure is more ... How much 3D structure knowledge do we have? *Primary and derived 3D structure databases. Structural Genomics: Worldwide Protein ...
  • The ribosome is probably the largest molecular machine, and is composed of many RNA and protein molecules. (
  • The number of subunits in a protein complex can often be determined by measuring the hydrodynamic molecular volume or mass of the intact complex, which requires native solution conditions. (
  • The function of proteins depends on their structure, and defining the structure of individual proteins is a large part of modern Biochemistry and Molecular Biology. (
  • Even such small proteins contain hundreds of atoms and have molecular weights of over 5000 Daltons (Da). (
  • This structure was used to determine the structure of the other form by molecular replacement. (
  • Most proteins with a molecular weight greater than 50,000 consist of two or more noncovalently-linked monomers. (
  • In addition to general chemistry texts, information about protein structure can be found in texts for biochemistry, organic chemistry, general biology, genetics, and molecular biology. (
  • Similarly, they can take into account the associated conservation at the molecular signatures level (SDPs) in fundamental regions corresponding to ligand-binding sites and protein interaction sites. (
  • The combination of results points to a molecular architecture formed by a rhombus-shaped heterotetramer, which is bound to two different interacting heterotrimeric G proteins (G i and G s ). (
  • Here, we propose a quaternary structure of a heteromer, taking into account the molecular stoichiometry and the interacting G proteins. (
  • Here, we have devised the molecular architecture of the adenosine A 1 R-A 2A R heteromer in complex with G proteins using a combination of microscope-based single-particle tracking, molecular modeling, and energy transfer assays in combination with molecular complementation. (
  • iii) Visualizing, as far as possible in frontal lessons, both molecular structure by the use of molecular models, and chemical compounds by the study of physical properties and laboratory techniques. (
  • His studies have provided insights into the relationship among hydration, molecular mobility and protein action. (
  • In silico gene reconstruction and molecular modelling indicate remarkable conservation of viral structure over a geologic timescale. (
  • Here we suggest a molecular mechanism for electromechanical coupling and gating polarity in non-domain-swapped K v channels on the basis of the cryo-electron microscopy structure of KAT1, the hyperpolarization-activated K v channel from Arabidopsis thaliana . (
  • Here we analyze the crystal structure of CSN5 in its catalytically inactive form to illuminate the molecular basis for its activation state. (
  • Each molecular structure has a specific energetic state. (
  • Insights on protein thermal stability: a graph representation of molecular interactions. (
  • First, a C-terminal catalytic site triggers an intra-molecular cleavage that releases the N-terminal portion of these proteins in the extracellular medium. (
  • Direct simulation of protein folding in atomic detail, via methods such as molecular dynamics with a suitable energy function, is typically not tractable due to the high computational cost, despite the efforts of distributed computing projects such as [email protected] . (
  • His research interests are mainly in protein molecular biology, particularly heterologous expression, quaternary structure and folding. (
  • Protein molecular biology. (
  • Molecular cloning of complementary DNA for the alpha subunit of the G protein that stimulates adenylate cyclase. (
  • Protein quaternary structure is the number and arrangement of multiple folded protein subunits in a multi-subunit complex. (
  • The quaternary structure refers to the number and arrangement of the protein subunits with respect to one another. (
  • Changes in quaternary structure can occur through conformational changes within individual subunits or through reorientation of the subunits relative to each other. (
  • The experiments often provide an estimate of the mass of the native protein and, together with knowledge of the masses and/or stoichiometry of the subunits, allow the quaternary structure to be predicted with a given accuracy. (
  • Tryptophan residues are commonly found in interfaces between proteins and their subunits, and histidines have been implicated in pH-dependent conformation changes. (
  • These proteins are called oligomers because they have two or more subunits. (
  • It is the spatial arrangement of subunits in a protein that consists of more than one polypeptide chain. (
  • 1. The most common number of subunits is either 2 (dimer) or 4 (tetramer), but trimers, pentamers, and hexadecamers and higher order structures also occur. (
  • Sickle Quaternary Ammonium Compounds Hemoglobin C Oxyhemoglobins Hemoglobin A, Glycosylated Hemoglobin E Methemoglobin Hemoglobin A2 Carboxyhemoglobin Amino Acids Truncated Hemoglobins Oxygen Heme Ligands Myoglobin … Quaternary structure is held together by noncovalent bonds between complementary surface hydrophobic and hydrophilic regions on the polypeptide subunits. (
  • The stabilizing forces that hold the polypeptide subunits together are the same forces that are responsible for tertiary structure stabilization. (
  • The overall 3D structure of a protein which is made up of multiple polypeptide chains (subunits), including how those subunits fit together, is the quaternary structure. (
  • 14 rue de Provigny 94236 Cachan cedex FRANCE Heures d'ouverture 08h30-12h30/13h30-17h30 The quaternary structure describes the arrangement and position of each of the subunits in a multiunit protein. (
  • The globular core of the molecule in different subunits in the two forms and those in Escherichia coli SSB (EcoSSB) and human mitochondrial SSB (HMtSSB) have similar structure, although the three loops exhibit considerable structural variation. (
  • Hemoglobin's quaternary structure is the package of its monomeric subunits. (
  • Because there are two different subunits, hemoglobin exhibits heteroquaternary structure. (
  • Hydrophobic interaction is the main stabilizing force for subunits in quaternary structure. (
  • The fourth level of protein structure that refers to the spatial arrangement of the subunits within the protein. (
  • Despite the demonstrated constitutive and functional importance of supramolecular assemblies of transmembrane subunits or proteins, effective tools for structure predictions of such assemblies are still lacking. (
  • A structural level wherein several proteins (or polypeptide subunits) interact through non-covalent bonds to form one functional protein complex. (
  • Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. (
  • For example, hemoglobin is a protein made up of four subunits, two α and two β . (
  • Type-specific regulation of adenylyl cyclase by G protein beta gamma subunits. (
  • When multiple copies of a polypeptide encoded by a gene form a quaternary complex, this protein structure is referred to as a multimer. (
  • The dimer structure of transcription factors is involved in gene regulation, but the trimer structure of virus-infection-associated glycoproteins is related to the human immunodeficiency virus. (
  • The sequence of amino acid residues in a protein is defined by the sequence of a gene , which is encoded in the genetic code . (
  • The one gene-one polypeptide hypothesis is an idea in an attempt to fix the one gene-one protein hypothesis (previously one gene-one enzyme hypothesis) after scientists realized that proteins can be made up by more than one polypeptide chain and that each polypeptide chain is specified by its own gene. (
  • Why was the one gene one protein hypothesis altered to one gene one polypeptide hypothesis? (
  • Because one gene codes for one polypeptide and some proteins are made of more than one polypeptide and stuck together after translation of the genes that code for these polypeptides. (
  • Not sure if there ever was a one gene one protein hypothesis or if its just something they teach in schools to avoid overcomplicating things. (
  • This hypothesis states that the function of an individual gene is to dictate the production of a specific enzyme.Since then, scientists have learned that some genes actually dictate the production of a single polypeptide, which may make up part of an enzyme or another kind of protein. (
  • A gene codes for one type of polypeptide (protein). (
  • The structure of protein families is shaped by the sequence divergence accumulated as a consequence of speciation, gene duplication, and deletion events, as well as by the evolutionary selective pressure exerted on each protein in accordance with the corresponding 3D structure and the specific function performed ( 1 , 2 ). (
  • This gene encodes a protein that functions as an assembly component of multiple structure-specific endonucleases. (
  • SLX4 (SLX4 Structure-Specific Endonuclease Subunit) is a Protein Coding gene. (
  • CUL5 (Cullin 5) is a Protein Coding gene. (
  • Gene Ontology (GO) annotations related to this gene include protein heterodimerization activity and ubiquitin protein ligase binding . (
  • The protein encoded by this gene is a high affinity calcium ion-binding protein that is structurally and functionally similar to calmodulin and troponin C. The encoded protein is thought to be involved in muscle relaxation. (
  • PVALB (Parvalbumin) is a Protein Coding gene. (
  • The low density lipoprotein receptor (LDLR) gene family consists of cell surface proteins involved in receptor-mediated endocytosis of specific ligands. (
  • LDLR (Low Density Lipoprotein Receptor) is a Protein Coding gene. (
  • This gene encodes a membrane protein belonging to the interleukin-17 receptor (IL-17R) protein family. (
  • IL17RD (Interleukin 17 Receptor D) is a Protein Coding gene. (
  • This gene encodes a member of the parvin family of actin-binding proteins. (
  • PARVA (Parvin Alpha) is a Protein Coding gene. (
  • This gene encodes a member of the bicoid subfamily of the paired (PRD) homeobox family of proteins. (
  • GSC (Goosecoid Homeobox) is a Protein Coding gene. (
  • The protein encoded by this gene is found in rod cells in the back of the eye and is essential for vision in low-light conditions. (
  • RHO (Rhodopsin) is a Protein Coding gene. (
  • GO annotations related to this gene include G-protein coupled receptor activity and photoreceptor activity . (
  • This gene encodes a secreted ligand of the TGF-beta (transforming growth factor-beta) superfamily of proteins. (
  • GDF6 (Growth Differentiation Factor 6) is a Protein Coding gene. (
  • Gene Ontology (GO) annotations related to this gene include protein homodimerization activity and growth factor activity . (
  • This gene encodes a member of the mucin protein family. (
  • The protein encoded by this gene is secreted and forms an insoluble mucous barrier that protects the gut lumen. (
  • MUC6 (Mucin 6, Oligomeric Mucus/Gel-Forming) is a Protein Coding gene. (
  • TBC1D28 (TBC1 Domain Family Member 28) is a Protein Coding gene. (
  • MTF2 (Metal Response Element Binding Transcription Factor 2) is a Protein Coding gene. (
  • MYH4 (Myosin Heavy Chain 4) is a Protein Coding gene. (
  • C1orf68 (Chromosome 1 Open Reading Frame 68) is a Protein Coding gene. (
  • ROR1 (Receptor Tyrosine Kinase Like Orphan Receptor 1) is a Protein Coding gene. (
  • Gene Ontology (GO) annotations related to this gene include transferase activity, transferring phosphorus-containing groups and protein tyrosine kinase activity . (
  • CALML3 (Calmodulin Like 3) is a Protein Coding gene. (
  • SLC22A24 (Solute Carrier Family 22 Member 24) is a Protein Coding gene. (
  • PLBD2 (Phospholipase B Domain Containing 2) is a Protein Coding gene. (
  • CACFD1 (Calcium Channel Flower Domain Containing 1) is a Protein Coding gene. (
  • Pharmacologic studies have determined that cysteinyl leukotrienes activate at least 2 receptors, the protein encoded by this gene and CYSLTR1. (
  • CYSLTR2 (Cysteinyl Leukotriene Receptor 2) is a Protein Coding gene. (
  • He teaches protein structure/function, gene expression and microbiology. (
  • A gene is a small portion of the genome - a sequence of nucleotides that is expressed together and codes for a single protein (polypeptide) molecule. (
  • For a gene to be expressed, i.e., translated into RNA , that portion of the DNA has to be uncoiled and freed of the protective proteins. (
  • RNA splicing allows for one gene to code for multiple related kinds of proteins, as alternative patterns of splicing may be controlled by various factors in the cell. (
  • The genetic code (nucleotide sequence of a gene) translates into a polypeptide (amino-acid sequence of a protein) in a 3-to-1 fashion. (
  • Homologies between signal transducing G proteins and ras gene products. (
  • It can also refer to biomolecular complexes of proteins with nucleic acids and other cofactors. (
  • The national center for biotechnology information's protein clusters database," Nucleic Acids Research , vol. 37, supplement 1, pp. (
  • The key biological molecules are carbohydrates, lipids, proteins and nucleic acids. (
  • Like other biological macromolecules such as polysaccharides and nucleic acids , proteins are essential parts of organisms and participate in virtually every process within cells . (
  • In this day of exploding bioinformatics information from genomics and proteomics, it is ever more important to be conversant with macromolecular three-dimensional structure, and how it relates to protein and nucleic acid function and drug design. (
  • The completion of the human genome project has opened a new area for studying nucleic acid and protein interactions using nucleic acid cross-linking reagents, and advances have also been made in the area of biosensors and microarray biochips for the detection and analysis of genes, proteins, and carbohydrates. (
  • ex: proteins, polysaccharides and nucleic acids. (
  • Many proteins are actually assemblies of multiple polypeptide chains. (
  • Disulfide bonding can form within and between polypeptide chains as proteins fold to its native conformation. (
  • The secondary structure of proteins where the polypeptide chains are almost completely extended during the process of folding. (
  • Additionally, some proteins form quaternary structures, assemblies of two or more polypeptide chains. (
  • The primary structure of a polypeptide of protein determines its secondary, tertiary, and quaternary structures. (
  • The biological functions of proteins are dependent on their tertiary and quaternary structures, and hence it is important to understand the determinants of quaternary association in proteins. (
  • M2 - explain the tertiary and quaternary structures of proteins. (
  • Modeling of Protein Tertiary and Quaternary Structures Based on Evolutionary Information. (
  • Primary, secondary, tertiary and quaternary structures of proteins. (
  • Levels of protein structure - quaternary Some proteins form assemblies (units) with other molecules - this is called the quaternary structure (Figure 14). (
  • Proteins are the largest and most varied class of biological molecules, and they show the greatest variety of structures. (
  • The aggregation of nonpolar side chains in the interior of a protein is favored by the increase in Entropy of the water molecules that would otherwise form cages around the hydrophobic groups. (
  • Proteins perform a vast array of functions within organisms , including catalysing metabolic reactions , DNA replication , responding to stimuli , providing structure to cells , and organisms , and transporting molecules from one location to another. (
  • Macromolecular Crystals: The Growth of Crystals Is Now the Key to Deducing the Structure of Large Molecules. (
  • Proteins are created from one or more of these polypeptide molecules. (
  • This quiz is based on the various aspects of the structure of protein molecules and amino acids. (
  • Proteins are polymer s whose molecules are made from many amino acid molecules linked together. (
  • A quaternary structure of a protein refers to the assembly of multiple folded protein molecules in a multi- subunit complex . (
  • Used by Structure Diagram and ViewDock to draw 2D diagrams of small organic molecules given coordinates or a SMILES string. (
  • The aim of the course is to provide the basis for interpreting and predicting the structure, physical properties and chemical behavior of organic molecules. (
  • Screening-based approaches to identify small molecules that inhibit protein-protein interactions. (
  • Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. (
  • Protein molecules that are attached to, or associated with the membrane of a cell or an organelle. (
  • Allows fetching modeled structures ( comparative models ) specified by SwissProt, TrEMBL, GenPept or PIR accession code. (
  • The atomic models of the KAT1 tetramer and octamer have been deposited in the Protein Data Bank under accession code 6V1X and 6V1Y , respectively. (
  • Serving as the basic structural molecule of all the tissues in the body, protein makes up nearly 17 percent of the total body weight. (
  • Secondary structure is the ordered arrangement or conformation of amino acids in localized regions of a polypeptide or protein molecule. (
  • Also, for a protein composed of a single polypeptide molecule, tertiary structure is the highest level of structure that is attained. (
  • Internet Explorer is OK but usually cannot display the Features of the Molecule control panel in Protein Explorer. (
  • its structure resulting from the union of more than one protein molecule, called subunit proteins. (
  • Allows fetching modeled organic molecule structures specified by PubChem CID. (
  • Generates modeled organic molecule structures specified by SMILES string with the command open or in Build Structure . (
  • The SMILES translator provided by the National Cancer Institute CADD group is used to generate 3D molecule structures specified by SMILES string with the command open or in Build Structure . (
  • The answer is due in part to the fact that O 2 is very poorly soluble in water (1.5 percent), and in part to the structure of the hemoglobin molecule itself. (
  • The encoded protein binds to 11-cis retinal and is activated when light hits the retinal molecule. (
  • Planar structure with rotational freedom within molecule found on alpha carbon. (
  • The proinsulin folds and binds to give the molecule its final structure. (
  • A major problem is that the protein is first synthesized as a linear molecule that subsequently must reach its native configuration in an extremely short time. (
  • In this concept the protein molecule is influenced by various long and short distance force fields of nature such as coherent electromagnetic waves and zero-point energy. (
  • A major problem (the so called Levinthal's paradox) is that the protein is first synthesized as a linear molecule that subsequently must reach its native configuration in a short time (on the order of seconds or less, Figure 1 ). (
  • The problem, however, is that the number of possible conformational states is exponentially large for a long protein molecule. (
  • This review outlines how the value of experimental data is optimized by combining high-quality protein sequences with complementary experimental results, including information derived from protein 3D-structures, using as an example the UniProt knowledgebase (UniProtKB) and the tools and links provided on its website ( ). (
  • The Universal Protein Resource KnowledgeBase (UniProtKB) ( ) provides the scientific community with one such resource. (
  • New protein sequences are integrated in UniProtKB/TrEMBL and annotated by an automated procedure. (
  • UniProtKB contains two mutually exclusive, non-redundant sections that together give access to all the protein sequences which are available to the public. (
  • Some bioinformatics methods were developed for predicting the quaternary structural attributes of proteins based on their sequence information by using various modes of pseudo amino acid composition. (
  • Primary structure is simply the sequence of residues making up the protein. (
  • So the primary structure of a small protein would consist of a sequence of 50 or so residues. (
  • A family of large surface proteins was identified, some associated with large amounts of non-coding repetitive DNA, and an unexpected degree of sequence variation. (
  • The sequence variation indicates both known and novel mechanisms for the elaboration and variation of surface structures, and suggests that immune evasion and host interaction play an important part in the lifestyle of this persistent bacterial pathogen. (
  • A 40% sequence identity filter is applied before the structure alignments are calculated, so most results show low similarity. (
  • Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes , and which usually results in protein folding into a specific three-dimensional structure that determines its activity. (
  • The primary structure of polypeptides and proteins is the sequence of amino acids in the polypeptide chain with reference to the locations of any disulfide bonds. (
  • The most common way to denote a primary structure is to write the amino acid sequence using the standard three-letter abbreviations for the amino acids. (
  • The first level of protein structure that is simply the linear sequence of its constituent amino acids. (
  • The second level of protein structure where the linear sequence of proteins begins to fold into regular repeating patterns. (
  • The unique three-dimensional structure of both monomeric and oligomeric proteins is encoded in their sequence. (
  • The present study, performed along with traditional sequence alignment methods, has provided the signature sequence motifs for different kinds of quaternary association seen in lectins. (
  • The primary structure of a protein is the sequence of amino acid s in the polypeptide (s). (
  • I tried to model a protein sequence (4 chains) using RosettaCM. (
  • The Blast Protein tool performs protein sequence searches using a BLAST Web service hosted by the UCSF Resource for Biocomputing, Visualization, and Informatics (RBVI) . (
  • Clicking the link to view results in Chimera displays the query structure and the multiple sequence alignment from ConSurf, both colored by the server's conservation measure. (
  • Choosing the "launch Chimera" option to show a modeled structure displays it along with the template structure and their pairwise sequence alignment. (
  • Chimera Web data files are provided for viewing enzyme structures, active sites (Chimera sessions), and sequence alignments. (
  • The "Chimera (Structure/Alignment)" option displays the modeled structure along with the template structure and the sequence alignment between the two. (
  • A user friendly web server, called PQSA-Pred , has been established at , by which one can predict the quaternary structural attributes of proteins according to their sequence information alone. (
  • Massive amounts of protein sequence data are produced by modern large-scale DNA sequencing efforts such as the Human Genome Project. (
  • The linear sequence of amino acids in the protein is its primary structure. (
  • Amino acids' unique sequence in a polypeptide chain is its primary structure. (
  • Translation of the DNA/RNA code into a sequence of amino-acids is just the beginning of the process of protein synthesis. (
  • Adenylyl cyclase amino acid sequence: possible channel- or transporter-like structure. (
  • Through the use of conformation-specific antibodies, we found that newly synthesized G protein folded into a conformation similar to the mature form within 1-3 min of synthesis and before trimer formation. (
  • Only proline differs from this basic structure as it contains an unusual ring to the N-end amine group, which forces the CO-NH amide moiety into a fixed conformation. (
  • The cruciform R structure is stabilized by a novel `leucine lock', which prevents the key residue, Asp187, from locking loop L2 in the disengaged conformation. (
  • In addition, the crystal structures of muscle FBPase in the T conformation with and without AMP strongly suggest that the T-to-R transition is a discrete jump rather than a shift of an equilibrium smooth transition through multiple intermediate states. (
  • His other contributions pertain to the structure and interactions of non-steroidal anti-inflammatory analgesics, ionophores and related compounds, side chain conformation in proteins and additional binding sites in lysozyme. (
  • To understand how the protein gets its final shape or conformation, we need to understand the four levels of protein structure: primary, secondary, tertiary, and quaternary. (
  • Long chains of amino acids, called polypeptides, make up the multicomponent, large complexes of protein. (
  • In the natural course of making a protein, polypeptides are elongated by the addition of amino acids to the C-terminal end of the growing chain. (
  • Short polypeptides, containing less than 20-30 residues, are rarely considered to be proteins and are commonly called peptides , or sometimes oligopeptides . (
  • There are four levels of structure found in polypeptides and proteins . (
  • Many polypeptides fold into compact, globular structures in which amino acid residues that are distant from each other in primary structure come into close proximity in the folded structure. (
  • For the first time, the structure of multi-subunit protein (immunoglobulin light chain) was solved in three crystal forms, differing only in the pH and ionic strength of the solvent of crystallization. (
  • Each polypeptide is referred to as a subunit of the protein. (
  • Here, we show by structural, biophysical, and enzymatic analyses combined with in vivo data that the class III Fic protein NmFic from Neisseria meningitidis gets autoadenylylated in cis , thereby autonomously relieving autoinhibition and thus allowing subsequent adenylylation of its target, the DNA gyrase subunit GyrB. (
  • Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. (
  • Functional evaluation of KAT1 structure-guided mutants at the sensor-pore interfaces suggests a mechanism in which direct interaction between the sensor and the C-linker hairpin in the adjacent pore subunit is the primary determinant of gating polarity. (
  • Splice variants of the alpha subunit of the G protein Gs activate both adenylyl cyclase and calcium channels. (
  • Structure determination of membrane proteins with magic angle spinning NMR is rapidly developing. (
  • The vesicular stomatitis virus glycoprotein (G protein) is an integral membrane protein which assembles into noncovalently associated trimers before transport from the endoplasmic reticulum. (
  • Several proteins inserted into the membrane participate in the transport of metabolites and ions. (
  • Benchmarks of the approach were done on ten homo-oligomeric membrane proteins with known quaternary structure. (
  • Collectively, the results of this study emphasize the effectiveness of the prediction protocol that will be extensively challenged in quaternary structure predictions of other integral membrane proteins. (
  • G-protein-coupled receptors (GPCRs), which constitute the largest superfamily of membrane proteins, are not exceptions to this rule. (
  • Herein, we present an approach based upon rigid body docking simulations, membrane topology-based filtering, and cluster analysis to predict the quaternary structure of homo-oligomeric integral membrane proteins. (
  • Projection maps of two different crystal forms of OmpG at 6 A resolution show that the protein has a beta-barrel structure characteristic for outer membrane proteins, and that it does not form trimers, unlike most other porins such as OmpF and OmpC, but appears in monomeric form. (
  • Bezanilla, F. How membrane proteins sense voltage. (
  • Low density lipoprotein (LDL) is normally bound at the cell membrane and taken into the cell ending up in lysosomes where the protein is degraded and the cholesterol is made available for repression of microsomal enzyme 3-hydro. (
  • Low density lipoprotein (LDL) is normally bound at the cell membrane and taken into the cell ending up in lysosomes where the protein is degraded and the cholesterol is made available for repression of microsomal enzyme 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) reductase, the rate-limiting step in cholesterol synthesis. (
  • The encoded protein is a glycosylated type I membrane protein that belongs to the ROR subfamily of cell surface receptors. (
  • They are recognized based on their common organization: they are comprised of an N-terminal, sec -dependent, signal-peptide required for targeting to- and export through the inner membrane, followed by a "passenger domain" (which is the functional, secreted part of the protein), and a C-terminal β-domain (or 'translocator" domain), which folds as a β-barrel in the outer membrane (OM). (
  • In contrast, proteins present in cell membranes often have hydrophobic amino acids on the surface that interact with glycerophospholipids in the membrane and have hydrophilic cores. (
  • The primary structure of each protein has been precisely determined by the specific genes. (
  • The major breakthrough in demonstrating the relationship between genes and proteins came in the 1940s. (
  • The typical AAV genome contains two protein-encoding genes termed rep and cap that, respectively, encode nonstructural proteins essential for viral genome replication and structural proteins that form the viral capsid. (
  • Cell uses the genes to synthetise proteins. (
  • The three resulting {open_quotes}snapshots{close_quotes} of possible structures show that their variable-domain interactions differ, reflecting their stabilities in specific solvent conditions. (
  • Protein structures are governed primarily by hydrophobic effects and by interactions between polar residues and other types of bonds. (
  • This will eliminate many of the ionic interactions that were necessary for maintenance of the folded shape of the protein. (
  • It is the different interactions between the side chains of the amino acids that stabilize the tertiary structure. (
  • The third level of protein structure where side chain interactions dictate the direction of the folding. (
  • Participants will be enabled to incorporate computer visualization and qualitative analysis of 3D structure of protein, DNA, RNA, and protein-ligand interactions into their teaching and research. (
  • We have systematically extended this observation to include the role of differential protein interactions in the segregation of protein subfamilies and explored in detail the structural distribution of SDPs at protein interfaces. (
  • Our results show the extensive influence of protein interactions in the evolution of protein families and the widespread association of SDPs with protein interfaces. (
  • Interestingly, even though specific protein interactions certainly are an important part of protein function, the organization of protein families in relation to the specific interactions of different subfamilies remains a poorly studied aspect of functional specificity. (
  • Notwithstanding, the information currently available on protein sequences, structures, functions, and interactions opens the door to performing more comprehensive studies of the relationships between family organization and functional divergence ( 17 ). (
  • its structure resulting from interactions between amino acid side chains. (
  • The crystal structure of the muscle-isozyme R form shows that in this arrangement of the tetramer completely new protein surfaces are exposed that are most likely targets for the interactions with various cellular and enzymatic partners. (
  • He has also contributed towards the area of structure and interactions of mycobacterial proteins and supramolecular association with reference to chemical evolution and origin of life. (
  • Such interfaces, especially of homologous but non-identical proteins, have been associated with biologically relevant interactions. (
  • The formation of the tertiary structure occurs due to interactions between the R-groups of the amino acids. (
  • The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain). (
  • The work on lectins demonstrated the need for considering open quaternary structures when dealing with multimeric proteins and the variability in the quaternary association of legume lectins. (
  • Examples of proteins with quaternary structure include hemoglobin, DNA polymerase, and ion channels. (
  • The most common example used to illustrate quaternary structure is the hemoglobin protein. (
  • An example would be a protein like hemoglobin, the oxygen transporting protein of vertebrate blood cells. (
  • An RBC's role is basically as a floating sack of hemoglobin , which is the protein that carries oxygen. (
  • The single-minded purpose of the cell is linked to the hemoglobin , or Hb , which makes up 95 percent of the proteins in the cell. (
  • The critical residues involved in the observed solvent response are tryptophans and histidines located between the two variable domains in the dimeric structure. (
  • Thus primary structure involves only the covalent bonds linking residues together. (
  • There is no theoretical maximum size, but the largest protein so far discovered has about 30,000 residues. (
  • Proteins are large biomolecules , or macromolecules , consisting of one or more long chains of amino acid residues . (
  • Shortly after or even during synthesis, the residues in a protein are often chemically modified by post-translational modification , which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. (
  • The lectin structure graphs have been used to obtain clusters of non-covalently interacting amino acid residues at the intersubunit interfaces. (
  • The present review also provides an overview of the methodology involved in representing oligomeric protein structures as connected networks of amino acid residues. (
  • The divergence accumulated during the evolution of protein families translates into their internal organization as subfamilies, and it is directly reflected in the characteristic patterns of differentially conserved residues. (
  • The most obvious example is the study of fully conserved positions that pinpoint important residues for the structure and function of the family members ( 5 ). (
  • Clicking a Chimera link displays the corresponding structure with nonsynonymous SNP residues (if any) shown with color and labeled with the dbSNP identifier. (
  • These cluster of hydrophobic residues in the center contributes to protein stability. (
  • Other assemblies referred to instead as multiprotein complexes also possess quaternary structure. (
  • More recently, people refer to protein-protein interaction when discussing quaternary structure of proteins and consider all assemblies of proteins as protein complexes. (
  • In our experiments we have observed evidence both of topologies that match what is known about protein assemblies in solution as well as discrete structural transitions that are only generated in the absence of bulk solvent. (
  • In this presentation, the gas-phase quaternary structures and structural transitions of protein assemblies that cover a range of known topologies in solution will be discussed. (
  • If the protein functioned as an enzyme denaturing will cause that protein to lose its enzymatic activity. (
  • Part of an enzyme needed for energy, and protein metabolism. (
  • Some proteins, such as haemoglobin , enzyme s and antibodies are involved in metabolic reactions, while others, such as collagen and keratin form the structure of living organisms. (
  • The quaternary structure of the enzyme, studied by Gas-phase Electrophoretic Mobility Macromolecule Analysis (GEMMA), was affected by addition of either single or both substrates in either direction of the reaction, resulting in a shift from UGPase dimers toward monomers, the active form of the enzyme. (
  • The substrate-induced changes in quaternary structure of the enzyme may have a regulatory role to assure maximal activity. (
  • As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. (
  • Myosins are a large family of motor proteins that share the common features of ATP hydrolysis (ATPase enzyme activity), actin binding and potential for kinetic energy transduction. (
  • Thereafter the middle section ('the C chain') of 33 amino-acids is removed by the action of the enzymes prohormone convertase 1 and 2, converting it into the final structure with 2 chains, A and B. Further 2 amino acids are removed by another enzyme carboxypeptidase E. (
  • If this active site is altered because of local changes or changes in overall protein structure, the enzyme may be unable to bind to the substrate. (
  • The above definition follows a classical approach to biochemistry, established at times when the distinction between a protein and a functional, proteinaceous unit was difficult to elucidate. (
  • After a Biochemistry degree, Ph.D. and Research Fellowship at the University of Cambridge, he moved to Imperial College London for further post-doctoral work in protein engineering. (
  • No known examples Although complexes higher than octamers are rarely observed for most proteins, there are some important exceptions. (
  • In some cases, proteins form complexes that then assemble into even larger complexes. (
  • This discussion will ultimately focus toward our long-term efforts to integrate ion mobility and mass spectrometry data in order to determine the topology and architecture of unknown protein complexes. (
  • Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes . (
  • This approach can also be used to probe the quaternary structure of protein complexes. (
  • These may include the global conservation of catalytic mechanisms (in the case of enzymes), specific binding to substrates and cofactors, as well as the interaction with other proteins in processes such as cell signaling, the regulation of reactions and the formation of macromolecular complexes. (
  • Core component of multiple SCF-like ECS (Elongin-Cullin 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. (
  • SWISS-MODEL: homology modelling of protein structures and complexes. (
  • Chemical structure of the peptide bond (bottom) and the three-dimensional structure of a peptide bond between an alanine and an adjacent amino acid (top/inset). (
  • Secondary Structures are the alpha helices and beta pleated sheets present in a folded protein's structure. (
  • Various types of secondary structures have been discovered, but by far the most common is the orderly repeating forms known as the a-helix and the b sheet. (
  • The two main secondary structures are the alpha helix and the anti-parallel beta-pleated sheet. (
  • A single polypeptide or protein may contain multiple secondary structures. (
  • Meets the grading criterias: P3 - describe the primary and secondary structures of proteins. (
  • The primary and secondary structures of the proteins determine which amino acids react with each other, and so determine just what the tertiary structure will be. (
  • Pattern Recognition in Sequences , Pattern Recognition in Secondary Structures , Pattern Recognition in Tertiary Structures, Pattern Recognition in Quaternary Structures, Pattern Recognition in Microarrays , Pattern Recognition in Phylogenetic Trees, and Pattern Recognition in Biological Networks . (
  • Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. (
  • representation is based upon the backbone, but highlights specific secondary structures (more on that later! (
  • The third level of structure, or tertiary structure, is how the secondary structures pack together to form the overall form of the entire peptide chain. (
  • Secondary structures form through hydrogen bonding between the oxygen from the carbonyl group of one amino acid and the hydrogen from the amino group of another. (
  • Common secondary structures include α -helices and β -pleated sheets. (
  • The arrangement of the monomers in the three-dimensional protein is the quaternary structure. (
  • If all of the monomers in a protein are identical, there is homoquaternary structure. (
  • What are the names for the monomers and polymers of proteins? (
  • G-protein-coupled receptors (GPCRs), in the form of monomers or homodimers that bind heterotrimeric G proteins, are fundamental in the transfer of extracellular stimuli to intracellular signaling pathways. (
  • We introduce a computational protocol for effective predictions of the supramolecular organization of integral transmembrane proteins, starting from the monomer. (
  • Surprisingly, the secondary structure and stability of the apo-monomer is indistinguishable from that of the M2-1 tetramer. (
  • The role of zinc goes beyond stabilization of local structure, finely tuning dissociation to a fully folded and binding competent monomer. (
  • Quaternary Protein - Structure The quaternary protein structure involves the clustering of several individual peptide or protein chains into a final specific shape. (
  • The side chains project outward and contact any solvent, producing a structure something like a bottle brush or a round hair brush. (
  • A major force stabilizing the tertiary structure is the hydrophobic interaction among nonpolar side chains in the core of the protein. (
  • The process whereby water-fearing protein side chains interact more favorably with themselves than with water to create a hydrophilic exterior. (
  • Proteins are organic compounds that are made up of one or more chains of amino acid. (
  • There are twenty different, naturally occurring amino acid s. amino acid s can link to form poly peptide chains and these can associate with one another to form proteins. (
  • The issue I am facing - the final modelled structure has all the 4 chains very far apart, unlike the pdb. (
  • Allows fetching protein sequences and their feature annotations by UniProt ID, either for PDB structure chains by PDB/UniProt Info , or independent of structure. (
  • The sequences of structure chains in Chimera can be submitted via the Align Chain Sequences tool, and/or sequences already in an alignment shown in Multalign Viewer can be submitted for realignment. (
  • In ProtCID, protein chains in the protein data bank (PDB) are grouped based on their PFAM domain architectures. (
  • Proteins are long chains of amino acids , and are synthesized by the ribosome , using messenger RNA as a template. (
  • These long chains form complicated structures that allow them to perform their function. (
  • Side chains play an important role in tertiary structure formation, especially the burying of hydrophobic ("water fearing") amino acids in the middle of the structure. (
  • as a result, oligomeric proteins can undergo rapid conformational changes that affect biological activity. (
  • The functional and biological significance of selected CASP13 targets are described by the authors of the structures. (
  • a protein that serves as a biological catalyst, changing the rate of a chemical reaction without itself being changed in the process. (
  • The current geometric and thermodynamic approaches in protein folding studies do not provide a definite solution to understanding mechanisms of folding of biological proteins. (
  • This recent finding of a set of discrete EM frequency bands, that either promote or endanger life conditions, could be a key in further studies directed at the morphogenetic aspects of protein folding in a biological evolutionary context. (
  • The SWISS-MODEL template library provides annotation of quaternary structure and essential ligands and co-factors to allow for building of complete structural models, including their oligomeric structure. (
  • Information about the oligomeric structure, ligands and cofactors is also provided. (
  • In this study we have examined the folding and oligomeric assembly of twelve mutant G proteins with alterations in the cytoplasmic, transmembrane, or ectodomains. (
  • This quaternary structure with a unique dimeric interface lends the oligomeric protein greater stability, which may be of significance to the functioning of the protein under conditions of stress. (
  • The above mentioned issues apply to all proteins, including well-behaving, small, monomeric proteins. (
  • Fibrous and globular proteins: characteristics and functions. (
  • D2 - discuss the relationship between the structure and function of proteins. (
  • Structure and function of proteins from primary to quaternary structures. (
  • In some proteins, the linear polypeptide chain is cross-linked: Disulfide bonds. (
  • Tertiary structure is largely maintained by disulfide bonds. (
  • Each of these 3-dimensional structures have three helices and three conserved disulfide bridges. (
  • If you are sure of the type of quaternary association, either from biochemical data and/or structural analysis of your model and its comparison to the template, it is relatively simple to apply the translational and rotational matrices to obtain a multimer. (
  • The biochemical properties of amino acids determine the role and function of protein in the human body. (
  • Many proteins are enzymes that catalyse biochemical reactions and are vital to metabolism . (
  • Indeed, such studies can involve biochemical function and protein interaction specificity. (
  • hRSV M2-1 is a tight tetramer bearing a Cys3-His1 zinc-binding motif, present in Ebola VP30 protein and some eukaryotic proteins, whose integrity was shown to be essential for protein function but without a biochemical mechanistic basis. (
  • A tale of tails: deciphering the contribution of terminal tails to the biochemical properties of two Dps proteins from Streptomyces coelicolor. (
  • Digestion breaks the proteins down for use in the metabolism. (
  • This level of structure describes the local folding pattern of the polypeptide backbone and is stabilized by hydrogen bonds between N-H and C=O groups. (
  • In a b sheet, the polypeptide chain folds back on itself so that polypeptide strands like side by side, and are held together by hydrogen bonds, forming a very rigid structure. (
  • Again, the polypeptide N-H and C=O groups form hydrogen bonds to stabilize the structure, but unlike the a-helix, these bonds are formed between neighbouring polypeptide (b) strands. (
  • Hydrogen bonds fine tune the tertiary structure by selecting the unique structure of a protein from among a relatively small number of hydrophobically stabilized conformations. (
  • Explanations of structural biology terms and concepts , e.g. asymmetric unit, Protein Data Bank, hydrogen bonds, temperature value, etc. all at About Macromolecular Structure . (
  • its structure resulting from hydrogen bonds between the C=O and N-H groups of different amino acids. (
  • These particular reactions between amino acids are hydrogen bonds , which create (relatively) small attractions between the "links" in the chain, which are nonetheless strong enough to determine if the protein will fold into sheets or twist into spirals . (
  • Many have intricate three-dimensional folding patterns that result in a compact form, but others do not fold up at all ("natively unstructured proteins") and exist in random conformations. (
  • To understand how proteins fold, we will start with the basics of structure, and progress through to structures of increasing complexity. (
  • The polypeptide chain in the structure exhibits the oligonucleotide binding fold. (
  • For example, proteins known as chaperones are required for some proteins to properly fold. (
  • Other proteins cannot fold properly without modifications such as glycosylation . (
  • Most proteins fold into specific three-dimensional structures to perform their function. (
  • SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. (
  • consist of a sufficient and balanced supply of both essential and nonessential amino acids in order to ensure high levels of protein production. (
  • Most proteins consist of linear polymers built from series of up to 20 different L -α- amino acids . (
  • Natural proteins consist of 100 to 500 building blocks (alpha-amino-acids), but a random search mechanism cannot provide real-time folding on the order of 1 sec. for these proteins. (
  • Protein structure homology modelling has become a routine technique to generate 3D models for proteins when experimental structures are not available. (
  • The database contains predicted protein structures from comparative (homology) modeling. (
  • Although the domain organization and, to a certain degree, the three-dimensional structure of autotransporters is conserved, their sequences show only weak homology. (
  • What are the main Functions of Proteins? (
  • This process of destroying the three-dimensional protein structure is called denaturation. (
  • what structure does denaturation destroy? (
  • Reversible and irreversible denaturation of proteins. (
  • Mad Cow Disease is a great way to get the students to pay attention before you lunge into the difficult lecture on protein synthesis (you start with prions, then work backwards). (
  • Rapid access to experiment-based information about well-characterized proteins helps predict the function of uncharacterized proteins identified by large-scale sequencing. (
  • Using computer modeling, aided by bioluminescence resonance energy transfer assays to monitor receptor homomerization and heteromerization and G-protein coupling, we predict the interacting interfaces and propose a quaternary structure of the GPCR tetramer in complex with two G proteins. (
  • In this link ( ) it is described as an application but I cannot understand how to make the system install it. (
  • Scientists can use the structure of a protein to predict its function and location in a cell. (
  • A representation of the 3-D structure of the protein myoglobin showing turquoise α-helices . (
  • The technological progress of the last few years has led to a literal explosion in the quantity of available data in life sciences, starting with the number of nucleotide and protein sequences, but also data from proteomic and transcriptomic studies. (
  • Much of the recent data are from large-scale studies, and most new nucleotide sequences code for otherwise uncharacterized proteins from a wide range of species, from mammals to microbes, virus isolates, and environmental samples. (
  • For the correct prediction of the function of individual proteins and for the automated annotation of entire genome sequences, one needs central knowledge resources that provide information about characterized proteins. (
  • Based on the homologies in the amino-acid sequences and the scattering profiles, these results are discussed in connection with the structures and function of LOV domains of phototropin. (
  • Multiple sequences alignments (MSAs) provide essential information on the evolution of protein families. (
  • Its aim is the prediction of the three-dimensional structure of proteins from their amino acid sequences, sometimes including additional relevant information such as the structures of related proteins. (
  • Despite community-wide efforts in structural genomics, the output of experimentally determined protein structures - typically by time-consuming and relatively expensive X-ray crystallography or NMR spectroscopy - is lagging far behind the output of protein sequences. (
  • The second level of structure is called secondary structure, and is the shapes (conformations) formed by short sequences of amino acids. (
  • The structural biologists discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submitted to the CASP13 experiment. (
  • FIC-domain enzymes are found in all kingdoms of life and catalyze posttranslational modifications of various target proteins to modulate their function. (
  • Filamentation induced by cyclic AMP (FIC)-domain enzymes catalyze adenylylation or other posttranslational modifications of target proteins to control their function. (
  • It is through such changes, which underlie cooperativity and allostery in "multimeric" enzymes, that many proteins undergo regulation and perform their physiological function. (
  • In this approach, enzymes are introduced in a limited amount with the strategy that the protein stereochemistry dictates the digestion rather than the enzymes specificity. (
  • Protein structure prediction is of high importance in medicine (for example, in drug design ) and biotechnology (for example, in the design of novel enzymes ). (
  • In cases where multiple alternative template structures are available for a protein of interest, a user-guided template selection step allows building models in different functional states. (
  • We used single-particle tracking experiments in cells expressing functional adenosine A 1 -A 2A receptors fused to fluorescent proteins to show the loss of Brownian movement of the A 1 receptor in the presence of the A 2A receptor, and a preponderance of cell surface 2:2 receptor heteromers (dimer of dimers). (
  • These amino acids - or, for practical purposes, (since all amino acids have certain functional group s in common) their remainder groups - determine what elements make up the protein, and in what quantities. (
  • The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. (
  • Classification of organic compounds: based on their structure and functional groups. (
  • Architectures and functional coverage of protein-protein interfaces. (
  • Hi Subhash First of all, you need to be sure that your model will have the same quaternary arrangement as your template. (
  • The arrangement of amino acids along the chain determines the structure and chemical properties of the protein. (
  • The tertiary structure of a polypeptide or protein is the three-dimensional arrangement of the atoms within a single polypeptide chain. (
  • H spin diffusion with MAS NMR is demonstrated for a helical transmembrane model protein complex. (
  • SLC22A24 belongs to a large family of transmembrane proteins that function as uniporters, symporters, and antiporters to transport organic ions across cell membranes (Jacobsson et al. (
  • Proteins are polymers of amino acids linked together through peptide bonds. (
  • For a polypeptide consisting of a single conformational folding pattern (e.g., an alpha helix only), the secondary and tertiary structure may be one and the same. (
  • Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal. (
  • Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors . (