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 characteristic three-dimensional shape of a molecule.
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.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
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.
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)
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A research technique to measure solvent exposed regions of molecules that is used to provide insight about PROTEIN CONFORMATION.
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.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Measurement of the intensity and quality of fluorescence.
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.
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.
The method of measuring the dispersion of an optically active molecule to determine the relative magnitude of right- or left-handed components and sometimes structural features of the molecule.
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).
The rate dynamics in chemical or physical systems.
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)
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.
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 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 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)
A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
A computer simulation developed to study the motion of molecules over a period of time.
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.
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.
Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light.
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)
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.
Computer-based representation of physical systems and phenomena such as chemical processes.
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.
A class of organic compounds which contain an anilino (phenylamino) group linked to a salt or ester of naphthalenesulfonic acid. They are frequently used as fluorescent dyes and sulfhydryl reagents.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
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.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Proteins prepared by recombinant DNA technology.
The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations.
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.
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.
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)
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.
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 3.2.1.17.
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
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.
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.
Small proteinaceous infectious particles which resist inactivation by procedures that modify NUCLEIC ACIDS and contain an abnormal isoform of a cellular protein which is a major and necessary component. The abnormal (scrapie) isoform is PrPSc (PRPSC PROTEINS) and the cellular isoform PrPC (PRPC PROTEINS). The primary amino acid sequence of the two isoforms is identical. Human diseases caused by prions include CREUTZFELDT-JAKOB SYNDROME; GERSTMANN-STRAUSSLER SYNDROME; and INSOMNIA, FATAL FAMILIAL.
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.
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)
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.
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)
The accumulation of an electric charge on a object
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)
Condensation products of aromatic amines and aldehydes forming azomethines substituted on the N atom, containing the general formula R-N:CHR. (From Grant & Hackh's Chemical Dictionary, 5th ed)
Proteins found in any species of bacterium.
A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease.
The study of PHYSICAL PHENOMENA and PHYSICAL PROCESSES as applied to living things.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The thermodynamic interaction between a substance and WATER.
Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest.
Deuterium. The stable isotope of hydrogen. It has one neutron and one proton in the nucleus.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
The physical characteristics and processes of biological systems.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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)
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 pressure due to the weight of fluid.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
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.
A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.
A type of FLUORESCENCE SPECTROSCOPY using two FLUORESCENT DYES with overlapping emission and absorption spectra, which is used to indicate proximity of labeled molecules. This technique is useful for studying interactions of molecules and PROTEIN FOLDING.
A group of genetic, infectious, or sporadic degenerative human and animal nervous system disorders associated with abnormal PRIONS. These diseases are characterized by conversion of the normal prion protein to an abnormal configuration via a post-translational process. In humans, these conditions generally feature DEMENTIA; ATAXIA; and a fatal outcome. Pathologic features include a spongiform encephalopathy without evidence of inflammation. The older literature occasionally refers to these as unconventional SLOW VIRUS DISEASES. (From Proc Natl Acad Sci USA 1998 Nov 10;95(23):13363-83)
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).
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
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.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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 serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
The process of cleaving a chemical compound by the addition of a molecule of water.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
The transfer of energy of a given form among different scales of motion. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed). It includes the transfer of kinetic energy and the transfer of chemical energy. The transfer of chemical energy from one molecule to another depends on proximity of molecules so it is often used as in techniques to measure distance such as the use of FORSTER RESONANCE ENERGY TRANSFER.
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 art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
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.
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)
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Proteins produced from GENES that have acquired MUTATIONS.
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.
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 3.4.21.4.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
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.
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.
Variation in a population's DNA sequence that is detected by determining alterations in the conformation of denatured DNA fragments. Denatured DNA fragments are allowed to renature under conditions that prevent the formation of double-stranded DNA and allow secondary structure to form in single stranded fragments. These fragments are then run through polyacrylamide gels to detect variations in the secondary structure that is manifested as an alteration in migration through the gels.
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.
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.
Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A type of scanning probe microscopy in which a probe systematically rides across the surface of a sample being scanned in a raster pattern. The vertical position is recorded as a spring attached to the probe rises and falls in response to peaks and valleys on the surface. These deflections produce a topographic map of the sample.
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
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.
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.
Analysis based on the mathematical function first formulated by Jean-Baptiste-Joseph Fourier in 1807. The function, known as the Fourier transform, describes the sinusoidal pattern of any fluctuating pattern in the physical world in terms of its amplitude and its phase. It has broad applications in biomedicine, e.g., analysis of the x-ray crystallography data pivotal in identifying the double helical nature of DNA and in analysis of other molecules, including viruses, and the modified back-projection algorithm universally used in computerized tomography imaging, etc. (From Segen, The Dictionary of Modern Medicine, 1992)
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.
Agents that emit light after excitation by light. The wave length of the emitted light is usually longer than that of the incident light. Fluorochromes are substances that cause fluorescence in other substances, i.e., dyes used to mark or label other compounds with fluorescent tags.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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.
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 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 characteristic 3-dimensional shape of a carbohydrate.
Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.
An essential amino acid. It is often added to animal feed.
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.
Established cell cultures that have the potential to propagate indefinitely.
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 species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539)
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 lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Sites on an antigen that interact with specific antibodies.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
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.
Antibodies produced by a single clone of cells.
That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.
A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
The sum of the weight of all the atoms in a molecule.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
Serum albumin from cows, commonly used in in vitro biological studies. (From Stedman, 25th ed)
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
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 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.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
Sequential operating programs and data which instruct the functioning of a digital computer.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)
Transport proteins that carry specific substances in the blood or across cell membranes.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Elements of limited time intervals, contributing to particular results or situations.
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.
A group of 13 or more deoxyribonucleotides in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties.
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
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 non-aqueous co-solvent that serves as tool to study protein folding. It is also used in various pharmaceutical, chemical and engineering applications.
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.
A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
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)
A representation, generally small in scale, to show the structure, construction, or appearance of something. (From Random House Unabridged Dictionary, 2d ed)
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
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.
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.
Proteins obtained from ESCHERICHIA COLI.
Layers of lipid molecules which are two molecules thick. Bilayer systems are frequently studied as models of biological membranes.
A group of deoxyribonucleotides (up to 12) in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties.
A site on an enzyme which upon binding of a modulator, causes the enzyme to undergo a conformational change that may alter its catalytic or binding properties.
The measurement of the quantity of heat involved in various processes, such as chemical reactions, changes of state, and formations of solutions, or in the determination of the heat capacities of substances. The fundamental unit of measurement is the joule or the calorie (4.184 joules). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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.
Pairing of purine and pyrimidine bases by HYDROGEN BONDING in double-stranded DNA or RNA.
The phenomenon whereby certain chemical compounds have structures that are different although the compounds possess the same elemental composition. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Disruption of the secondary structure of nucleic acids by heat, extreme pH or chemical treatment. Double strand DNA is "melted" by dissociation of the non-covalent hydrogen bonds and hydrophobic interactions. Denatured DNA appears to be a single-stranded flexible structure. The effects of denaturation on RNA are similar though less pronounced and largely reversible.
Peptides composed of between two and twelve amino acids.
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 monomeric units from which DNA or RNA polymers are constructed. They consist of a purine or pyrimidine base, a pentose sugar, and a phosphate group. (From King & Stansfield, A Dictionary of Genetics, 4th 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.
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.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
A polynucleotide consisting essentially of chains with a repeating backbone of phosphate and ribose units to which nitrogenous bases are attached. RNA is unique among biological macromolecules in that it can encode genetic information, serve as an abundant structural component of cells, and also possesses catalytic activity. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
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.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
An essential amino acid that is required for the production of HISTAMINE.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
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.
The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.
A group of peptide antibiotics from BACILLUS brevis. Gramicidin C or S is a cyclic, ten-amino acid polypeptide and gramicidins A, B, D are linear. Gramicidin is one of the two principal components of TYROTHRICIN.
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.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
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.
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
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)
The property of emitting radiation while being irradiated. The radiation emitted is usually of longer wavelength than that incident or absorbed, e.g., a substance can be irradiated with invisible radiation and emit visible light. X-ray fluorescence is used in diagnosis.
Measurement of the polarization of fluorescent light from solutions or microscopic specimens. It is used to provide information concerning molecular size, shape, and conformation, molecular anisotropy, electronic energy transfer, molecular interaction, including dye and coenzyme binding, and the antigen-antibody reaction.
Conformational transitions of the shape of a protein to various unfolded states.
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
The deductive study of shape, quantity, and dependence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
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 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.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
Circular duplex DNA isolated from viruses, bacteria and mitochondria in supercoiled or supertwisted form. This superhelical DNA is endowed with free energy. During transcription, the magnitude of RNA initiation is proportional to the DNA superhelicity.
A computer simulation technique that is used to model the interaction between two molecules. Typically the docking simulation measures the interactions of a small molecule or ligand with a part of a larger molecule such as a protein.

Endocytosis: EH domains lend a hand. (1/52898)

A number of proteins that have been implicated in endocytosis feature a conserved protein-interaction module known as an EH domain. The three-dimensional structure of an EH domain has recently been solved, and is likely to presage significant advances in understanding molecular mechanisms of endocytosis.  (+info)

Membrane fusion: structure snared at last. (2/52898)

The structure of the core of the neuronal 'SNARE complex', involved in neurotransmitter release, has been determined recently. Its topological similarity to viral fusion proteins suggests how the SNARE complex might facilitate membrane fusion.  (+info)

Four dimers of lambda repressor bound to two suitably spaced pairs of lambda operators form octamers and DNA loops over large distances. (3/52898)

Transcription factors that are bound specifically to DNA often interact with each other over thousands of base pairs [1] [2]. Large DNA loops resulting from such interactions have been observed in Escherichia coli with the transcription factors deoR [3] and NtrC [4], but such interactions are not, as yet, well understood. We propose that unique protein complexes, that are not present in solution, may form specifically on DNA. Their uniqueness would make it possible for them to interact tightly and specifically with each other. We used the repressor and operators of coliphage lambda to construct a model system in which to test our proposition. lambda repressor is a dimer at physiological concentrations, but forms tetramers and octamers at a hundredfold higher concentration. We predict that two lambda repressor dimers form a tetramer in vitro when bound to two lambda operators spaced 24 bp apart and that two such tetramers interact to form an octamer. We examined, in vitro, relaxed circular plasmid DNA in which such operator pairs were separated by 2,850 bp and 2,470 bp. Of these molecules, 29% formed loops as seen by electron microscopy (EM). The loop increased the tightness of binding of lambda repressor to lambda operator. Consequently, repression of the lambda PR promoter in vivo was increased fourfold by the presence of a second pair of lambda operators, separated by a distance of 3,600 bp.  (+info)

Probing interactions between HIV-1 reverse transcriptase and its DNA substrate with backbone-modified nucleotides. (4/52898)

BACKGROUND: To gain a molecular understanding of a biochemical process, the crystal structure of enzymes that catalyze the reactions involved is extremely helpful. Often the question arises whether conformations obtained in this way appropriately reflect the reactivity of enzymes, however. Rates that characterize transitions are therefore compulsory experiments for the elucidation of the reaction mechanism. Such experiments have been performed for the reverse transcriptase of the type 1 human immunodeficiency virus (HIV-1 RT). RESULTS: We have developed a methodology to monitor the interplay between HIV-1 RT and its DNA substrate. To probe the protein-DNA interactions, the sugar backbone of one nucleotide was modified by a substituent that influenced the efficiency of the chain elongation in a characteristic way. We found that strand elongation after incorporation of the modified nucleotide follows a discontinuous efficiency for the first four nucleotides. The reaction efficiencies could be correlated with the distance between the sugar substituent and the enzyme. The model was confirmed by kinetic experiments with HIV-1 RT mutants. CONCLUSIONS: Experiments with HIV-1 RT demonstrate that strand-elongation efficiency using a modified nucleotide correlates well with distances between the DNA substrate and the enzyme. The functional group at the modified nucleotides acts as an 'antenna' for steric interactions that changes the optimal transition state. Kinetic experiments in combination with backbone-modified nucleotides can therefore be used to gain structural information about reverse transcriptases and DNA polymerases.  (+info)

A hyperstable collagen mimic. (5/52898)

BACKGROUND: Collagen is the most abundant protein in animals. Each polypeptide chain of collagen is composed of repeats of the sequence: Gly-X-Y, where X and Y are often L-proline (Pro) and 4(R)-hydroxy-L-proline (Hyp) residues, respectively. These chains are wound into tight triple helices of great stability. The hydroxyl group of Hyp residues contributes much to this conformational stability. The existing paradigm is that this stability arises from interstrand hydrogen bonds mediated by bridging water molecules. This model was tested using chemical synthesis to replace Hyp residues with 4(R)-fluoro-L-proline (Flp) residues. The fluorine atom in Flp residues does not form hydrogen bonds but does elicit strong inductive effects. RESULTS: Replacing the Hyp residues in collagen with Flp residues greatly increases triple-helical stability. The free energy contributed by the fluorine atom in Flp residues is twice that of the hydroxyl group in Hyp residues. The stability of the Flp-containing triple helix far exceeds that of any untemplated collagen mimic of similar size. CONCLUSIONS: Bridging water molecules contribute little to collagen stability. Rather, collagen stability relies on previously unappreciated inductive effects. Collagen mimics containing fluorine or other appropriate electron-withdrawing substituents could be the basis of new biomaterials for restorative therapies.  (+info)

How do peptide synthetases generate structural diversity? (6/52898)

Many low-molecular-weight peptides of microbial origin are synthesized nonribosomally on large multifunctional proteins, termed peptide synthetases. These enzymes contain repeated building blocks in which several defined domains catalyze specific reactions of peptide synthesis. The order of these domains within the enzyme determines the sequence and structure of the peptide product.  (+info)

Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. (7/52898)

The lysosomal cysteine proteases cathepsins S and L play crucial roles in the degradation of the invariant chain during maturation of MHC class II molecules and antigen processing. The p41 form of the invariant chain includes a fragment which specifically inhibits cathepsin L but not S. The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L. The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges. The first subdomain is an alpha-helix-beta-strand arrangement, whereas the second subdomain has a predominantly beta-strand arrangement. The wedge shape and three-loop arrangement of the p41 fragment bound to the active site cleft of cathepsin L are reminiscent of the inhibitory edge of cystatins, thus demonstrating the first example of convergent evolution observed in cysteine protease inhibitors. However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites. This enables inhibitors based on the thyroglobulin type-1 domain fold, in contrast to the rather non-selective cystatins, to exhibit specificity for their target enzymes.  (+info)

Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D. (8/52898)

The crystal structure of profactor D, determined at 2.1 A resolution with an Rfree and an R-factor of 25.1 and 20.4%, respectively, displays highly flexible or disordered conformation for five regions: N-22, 71-76, 143-152, 187-193 and 215-223. A comparison with the structure of its mature serine protease, complement factor D, revealed major conformational changes in the similar regions. Comparisons with the zymogen-active enzyme pairs of chymotrypsinogen, trypsinogen and prethrombin-2 showed a similar distribution of the flexible regions. However, profactor D is the most flexible of the four, and its mature enzyme displays inactive, self-inhibited active site conformation. Examination of the surface properties of the N-terminus-binding pocket indicates that Ile16 may play the initial positioning role for the N-terminus, and Leu17 probably also helps in inducing the required conformational changes. This process, perhaps shared by most chymotrypsinogen-like zymogens, is followed by a factor D-unique step, the re-orientation of an external Arg218 to an internal position for salt-bridging with Asp189, leading to the generation of the self-inhibited factor D.  (+info)

Proteins are complex biomolecules made up of amino acids that play a crucial role in many biological processes in the human body. In the medical field, proteins are studied extensively as they are involved in a wide range of functions, including: 1. Enzymes: Proteins that catalyze chemical reactions in the body, such as digestion, metabolism, and energy production. 2. Hormones: Proteins that regulate various bodily functions, such as growth, development, and reproduction. 3. Antibodies: Proteins that help the immune system recognize and neutralize foreign substances, such as viruses and bacteria. 4. Transport proteins: Proteins that facilitate the movement of molecules across cell membranes, such as oxygen and nutrients. 5. Structural proteins: Proteins that provide support and shape to cells and tissues, such as collagen and elastin. Protein abnormalities can lead to various medical conditions, such as genetic disorders, autoimmune diseases, and cancer. Therefore, understanding the structure and function of proteins is essential for developing effective treatments and therapies for these conditions.

Silica gel is a desiccant, which is a substance that absorbs moisture from the air. It is commonly used in the medical field to remove moisture from medical equipment, such as syringes, vials, and other medical devices, to prevent the growth of bacteria and other microorganisms that thrive in moist environments. Silica gel is also used in the production of certain medications, such as insulin, to maintain the stability and potency of the medication. In addition, silica gel is sometimes used in wound dressings to absorb excess moisture and promote healing.

Myoglobin is a protein found in muscle tissue that plays a crucial role in oxygen storage and delivery. It is responsible for storing oxygen in muscle cells and releasing it when needed during periods of high physical activity. Myoglobin is also involved in the regulation of muscle metabolism and the removal of waste products from muscle cells. In the medical field, myoglobin levels are often measured in blood tests to diagnose and monitor various conditions, including muscle injuries, heart attacks, and kidney disease. High levels of myoglobin in the blood can indicate muscle damage or injury, while low levels may suggest a problem with muscle metabolism or oxygen delivery. Myoglobinuria, a condition characterized by the presence of myoglobin in the urine, can also be a sign of muscle injury or disease.

Tryptophan is an essential amino acid that is required for the production of proteins in the body. It is also a precursor to the neurotransmitter serotonin, which plays a role in regulating mood, appetite, and sleep. In the medical field, tryptophan is often used to treat conditions such as depression, anxiety, and insomnia. It is also used to help manage symptoms of premenstrual syndrome (PMS) and to improve athletic performance. Tryptophan supplements are available over-the-counter, but it is important to talk to a healthcare provider before taking them, as they can interact with certain medications and may have side effects.

Anilino naphthalenesulfonates are a class of organic compounds that are used in various medical applications. They are typically synthesized by the reaction of naphthalene-1-sulfonic acid with aniline or substituted anilines. These compounds have a planar aromatic structure and are often used as dyes, pigments, and surfactants. In the medical field, anilino naphthalenesulfonates are used as antimalarial agents. They are effective against Plasmodium falciparum, the parasite responsible for the most severe form of malaria. Some examples of anilino naphthalenesulfonates used in this context include chloroquine and hydroxychloroquine. Anilino naphthalenesulfonates are also used as antiviral agents. They have been shown to be effective against a variety of viruses, including influenza, herpes simplex virus, and human immunodeficiency virus (HIV). Some examples of anilino naphthalenesulfonates used in this context include amantadine and rimantadine. In addition to their antimalarial and antiviral properties, anilino naphthalenesulfonates have also been studied for their potential use in the treatment of other medical conditions, such as cancer and inflammatory diseases. However, more research is needed to fully understand their therapeutic potential and to develop safe and effective treatments based on these compounds.

Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.

In the medical field, peptides are short chains of amino acids that are linked together by peptide bonds. They are typically composed of 2-50 amino acids and can be found in a variety of biological molecules, including hormones, neurotransmitters, and enzymes. Peptides play important roles in many physiological processes, including growth and development, immune function, and metabolism. They can also be used as therapeutic agents to treat a variety of medical conditions, such as diabetes, cancer, and cardiovascular disease. In the pharmaceutical industry, peptides are often synthesized using chemical methods and are used as drugs or as components of drugs. They can be administered orally, intravenously, or topically, depending on the specific peptide and the condition being treated.

In the medical field, water is a vital substance that is essential for the proper functioning of the human body. It is a clear, odorless, tasteless liquid that makes up the majority of the body's fluids, including blood, lymph, and interstitial fluid. Water plays a crucial role in maintaining the body's temperature, transporting nutrients and oxygen to cells, removing waste products, and lubricating joints. It also helps to regulate blood pressure and prevent dehydration, which can lead to a range of health problems. In medical settings, water is often used as a means of hydration therapy for patients who are dehydrated or have fluid imbalances. It may also be used as a diluent for medications or as a component of intravenous fluids. Overall, water is an essential component of human health and plays a critical role in maintaining the body's normal functions.

Muramidase is an enzyme that is involved in the degradation of peptidoglycan, a major component of bacterial cell walls. It is also known as lysozyme or muramidase lysozyme. The enzyme cleaves the bond between the N-acetylglucosamine and N-acetylmuramic acid residues in the peptidoglycan chain, leading to the breakdown of the cell wall and ultimately the death of the bacterium. Muramidase is found in various organisms, including humans, and is used as an antimicrobial agent in some medications. It is also used in laboratory research to study bacterial cell wall structure and function.

Apoproteins are proteins that are associated with lipids (fats) in the bloodstream. They play a crucial role in the transport and metabolism of lipids in the body. There are several different types of apolipoproteins, each with a specific function. Apolipoproteins are found in lipoprotein particles, which are complexes of lipids and proteins that transport lipids through the bloodstream. The different types of apolipoproteins are associated with different types of lipoproteins, such as low-density lipoprotein (LDL) and high-density lipoprotein (HDL). Apolipoproteins are important for maintaining healthy lipid levels in the body. For example, HDL, which is often referred to as "good cholesterol," contains the apolipoprotein A-I, which helps to remove excess cholesterol from the bloodstream and transport it back to the liver for processing and elimination. Abnormal levels of apolipoproteins can be associated with various health conditions, such as high cholesterol, heart disease, and diabetes. Therefore, measuring levels of apolipoproteins can be an important part of diagnosing and managing these conditions.

In the medical field, hydrogen is not typically used as a standalone treatment or medication. However, there is some research being conducted on the potential therapeutic uses of hydrogen gas (H2) in various medical conditions. One area of interest is in the treatment of oxidative stress and inflammation, which are underlying factors in many chronic diseases such as cancer, diabetes, and neurodegenerative disorders. Hydrogen gas has been shown to have antioxidant and anti-inflammatory effects, and some studies have suggested that it may have potential as a therapeutic agent in these conditions. Another area of research is in the treatment of traumatic brain injury (TBI). Hydrogen gas has been shown to reduce oxidative stress and inflammation in animal models of TBI, and some studies have suggested that it may have potential as a neuroprotective agent in humans. However, it's important to note that the use of hydrogen gas in medicine is still in the early stages of research, and more studies are needed to fully understand its potential therapeutic benefits and risks. As such, hydrogen gas should not be used as a substitute for conventional medical treatments without the guidance of a qualified healthcare professional.

Prions are infectious agents that consist solely of protein, without any genetic material such as DNA or RNA. They are responsible for a group of rare and fatal neurodegenerative diseases, including Creutzfeldt-Jakob disease (CJD) and kuru in humans, and scrapie in sheep. Prions are unique in that they can cause normal proteins in the body to misfold and adopt the same abnormal shape, leading to the accumulation of these misfolded proteins in the brain and other tissues. This accumulation of misfolded proteins is what causes the damage and death of brain cells in prion diseases. Prions are highly resistant to heat, radiation, and many disinfectants, making them difficult to eliminate from contaminated materials. They can also be transmitted through contact with infected tissues or bodily fluids, or through contaminated food or medical equipment.

Guanidine is a chemical compound that is commonly used in the medical field as a medication and a research tool. It is a white, crystalline solid that is soluble in water and has a bitter taste. Guanidine is used to treat a variety of conditions, including hypertension (high blood pressure), congestive heart failure, and certain types of kidney disease. It works by relaxing blood vessels and reducing the workload on the heart, which can help to lower blood pressure and improve blood flow. Guanidine is also used in research to study the structure and function of proteins, and to develop new drugs and therapies.

Bacteriorhodopsins are a family of light-sensitive proteins found in the membranes of certain bacteria, such as Halobacterium salinarum. They are also known as light-driven proton pumps because they use the energy from light to pump protons across the membrane, creating a proton gradient that can be used to power various cellular processes. In the medical field, bacteriorhodopsins have been studied for their potential use in a variety of applications, including as optogenetic tools for controlling the activity of neurons in the brain, as sensors for detecting environmental pollutants, and as components of biofuel cells that can convert light energy into electrical energy. Bacteriorhodopsins have also been used in the development of new drugs and therapies. For example, researchers have developed a bacteriorhodopsin-based drug that can be used to treat glaucoma by increasing the production of aqueous humor in the eye. Additionally, bacteriorhodopsins have been used to develop new types of solar cells that can convert light energy into electrical energy more efficiently than traditional solar cells.

In the medical field, Schiff bases are a class of organic compounds that are formed by the condensation reaction between an amine and a carbonyl compound. These compounds are named after the German chemist Hugo Schiff, who first described their synthesis in the late 19th century. Schiff bases have a wide range of applications in medicine, including as antibacterial, antifungal, and antiviral agents. They are also used as ligands in metal complexes, which can be used in the treatment of various diseases, such as cancer and inflammatory disorders. One of the most well-known Schiff bases in medicine is metronidazole, which is used to treat infections caused by anaerobic bacteria and protozoa. Other examples of Schiff bases with medical applications include thiosemicarbazones, which are used to treat cancer, and salicylaldehyde Schiff bases, which have anti-inflammatory properties. Overall, Schiff bases are an important class of compounds in the medical field, with a wide range of potential applications in the treatment of various diseases and conditions.

Bacterial proteins are proteins that are synthesized by bacteria. They are essential for the survival and function of bacteria, and play a variety of roles in bacterial metabolism, growth, and pathogenicity. Bacterial proteins can be classified into several categories based on their function, including structural proteins, metabolic enzymes, regulatory proteins, and toxins. Structural proteins provide support and shape to the bacterial cell, while metabolic enzymes are involved in the breakdown of nutrients and the synthesis of new molecules. Regulatory proteins control the expression of other genes, and toxins can cause damage to host cells and tissues. Bacterial proteins are of interest in the medical field because they can be used as targets for the development of antibiotics and other antimicrobial agents. They can also be used as diagnostic markers for bacterial infections, and as vaccines to prevent bacterial diseases. Additionally, some bacterial proteins have been shown to have therapeutic potential, such as enzymes that can break down harmful substances in the body or proteins that can stimulate the immune system.

Amyloid is a type of protein that is abnormal and forms deposits in tissues throughout the body. These deposits are made up of fibrils, which are long, twisted strands of protein. Amyloidosis is a disease that occurs when amyloid fibrils build up in tissues, leading to damage and dysfunction. There are many different types of amyloidosis, which can affect different organs and tissues in the body. Some types of amyloidosis are inherited, while others are acquired. Treatment for amyloidosis depends on the specific type and severity of the disease.

Deuterium is a stable isotope of hydrogen that has one extra neutron in its nucleus compared to the most common isotope of hydrogen, protium. In the medical field, deuterium is sometimes used as a tracer in nuclear medicine imaging studies. For example, deuterium oxide (heavy water) can be used to label certain molecules, such as glucose or amino acids, which can then be injected into the body and imaged using positron emission tomography (PET) or single-photon emission computed tomography (SPECT). This can help doctors to visualize the uptake and metabolism of these molecules in different tissues and organs, which can be useful for diagnosing and monitoring various medical conditions. Deuterium is also used in some types of radiation therapy, where it is used to replace hydrogen atoms in certain molecules to make them more radioactive, allowing them to be targeted to specific cancer cells.

In the medical field, a peptide fragment refers to a short chain of amino acids that are derived from a larger peptide or protein molecule. Peptide fragments can be generated through various techniques, such as enzymatic digestion or chemical cleavage, and are often used in diagnostic and therapeutic applications. Peptide fragments can be used as biomarkers for various diseases, as they may be present in the body at elevated levels in response to specific conditions. For example, certain peptide fragments have been identified as potential biomarkers for cancer, neurodegenerative diseases, and cardiovascular disease. In addition, peptide fragments can be used as therapeutic agents themselves. For example, some peptide fragments have been shown to have anti-inflammatory or anti-cancer properties, and are being investigated as potential treatments for various diseases. Overall, peptide fragments play an important role in the medical field, both as diagnostic tools and as potential therapeutic agents.

In the medical field, macromolecular substances refer to large molecules that are composed of repeating units, such as proteins, carbohydrates, lipids, and nucleic acids. These molecules are essential for many biological processes, including cell signaling, metabolism, and structural support. Macromolecular substances are typically composed of thousands or even millions of atoms, and they can range in size from a few nanometers to several micrometers. They are often found in the form of fibers, sheets, or other complex structures, and they can be found in a variety of biological tissues and fluids. Examples of macromolecular substances in the medical field include: - Proteins: These are large molecules composed of amino acids that are involved in a wide range of biological functions, including enzyme catalysis, structural support, and immune response. - Carbohydrates: These are molecules composed of carbon, hydrogen, and oxygen atoms that are involved in energy storage, cell signaling, and structural support. - Lipids: These are molecules composed of fatty acids and glycerol that are involved in energy storage, cell membrane structure, and signaling. - Nucleic acids: These are molecules composed of nucleotides that are involved in genetic information storage and transfer. Macromolecular substances are important for many medical applications, including drug delivery, tissue engineering, and gene therapy. Understanding the structure and function of these molecules is essential for developing new treatments and therapies for a wide range of diseases and conditions.

Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of rare and fatal neurological disorders that are caused by abnormal proteins called prions. These diseases are characterized by the accumulation of misfolded prion proteins in the brain, leading to the destruction of brain tissue and the development of spongy holes, or vacuoles, in the brain. There are several different types of prion diseases, including Creutzfeldt-Jakob disease (CJD), kuru, Gerstmann-Sträussler-Scheinker syndrome (GSS), fatal familial insomnia (FFI), and variant Creutzfeldt-Jakob disease (vCJD). These diseases can affect humans and other animals, including cattle, sheep, and deer. Prion diseases are infectious, meaning that they can be transmitted from one individual to another through contact with infected tissues or bodily fluids. They are also unique in that they are not caused by viruses or bacteria, but rather by abnormal proteins. There is currently no cure for prion diseases, and treatment is focused on managing symptoms and providing supportive care.

DNA, or deoxyribonucleic acid, is a molecule that carries genetic information in living organisms. It is composed of four types of nitrogen-containing molecules called nucleotides, which are arranged in a specific sequence to form the genetic code. In the medical field, DNA is often studied as a tool for understanding and diagnosing genetic disorders. Genetic disorders are caused by changes in the DNA sequence that can affect the function of genes, leading to a variety of health problems. By analyzing DNA, doctors and researchers can identify specific genetic mutations that may be responsible for a particular disorder, and develop targeted treatments or therapies to address the underlying cause of the condition. DNA is also used in forensic science to identify individuals based on their unique genetic fingerprint. This is because each person's DNA sequence is unique, and can be used to distinguish one individual from another. DNA analysis is also used in criminal investigations to help solve crimes by linking DNA evidence to suspects or victims.

In the medical field, protons are subatomic particles that have a positive charge and are found in the nucleus of an atom. They are one of the two types of particles that make up atomic nuclei, the other being neutrons, which have no charge. Protons are important in medical applications because they can be used in a type of radiation therapy called proton therapy. Proton therapy is a type of cancer treatment that uses beams of protons to target and destroy cancer cells while minimizing damage to surrounding healthy tissue. This is because protons have a unique property called the Bragg peak, which allows them to deposit most of their energy at a specific depth in the body before coming to a stop. This makes proton therapy particularly effective for treating certain types of cancer, such as brain tumors and pediatric cancers.

Chymotrypsin is a digestive enzyme that is produced by the pancreas and secreted into the small intestine. It is a protease enzyme that breaks down proteins into smaller peptides and amino acids. Chymotrypsin is particularly effective at breaking down proteins that contain aromatic amino acids such as tryptophan, tyrosine, and phenylalanine. In the medical field, chymotrypsin is used to treat a variety of conditions, including: 1. Pancreatitis: Chymotrypsin is used to help break down the excess enzymes in the pancreas that can cause inflammation and damage to the pancreas. 2. Gallstones: Chymotrypsin is used to dissolve gallstones that are composed of cholesterol. 3. Inflammatory bowel disease: Chymotrypsin is used to help reduce inflammation in the digestive tract. 4. Cancer: Chymotrypsin is being studied as a potential treatment for certain types of cancer, including breast cancer and prostate cancer. Chymotrypsin is usually administered as a medication in the form of a tablet or injection. It is important to note that chymotrypsin can have side effects, including nausea, vomiting, and diarrhea, and should only be used under the guidance of a healthcare professional.

In the medical field, amides are a class of organic compounds that contain a nitrogen atom bonded to two carbon atoms. They are commonly used as drugs and are often referred to as "amide derivatives." One example of an amide derivative used in medicine is acetaminophen, which is commonly sold under the brand name Tylenol. It is used to relieve pain and reduce fever. Another example is aspirin, which is also an amide derivative and is used to relieve pain, reduce fever, and thin the blood. Amides can also be used as local anesthetics, such as lidocaine, which is used to numb the skin and nerves during medical procedures. They can also be used as muscle relaxants, such as succinylcholine, which is used to relax muscles during surgery. Overall, amides play an important role in medicine as they have a wide range of therapeutic applications and are often used to treat various medical conditions.

Cysteine is an amino acid that is essential for the proper functioning of the human body. It is a sulfur-containing amino acid that is involved in the formation of disulfide bonds, which are important for the structure and function of many proteins. Cysteine is also involved in the detoxification of harmful substances in the body, and it plays a role in the production of glutathione, a powerful antioxidant. In the medical field, cysteine is used to treat a variety of conditions, including respiratory infections, kidney stones, and cataracts. It is also used as a dietary supplement to support overall health and wellness.

In the medical field, a mutant protein refers to a protein that has undergone a genetic mutation, resulting in a change in its structure or function. Mutations can occur in the DNA sequence that codes for a protein, leading to the production of a protein with a different amino acid sequence than the normal, or wild-type, protein. Mutant proteins can be associated with a variety of medical conditions, including genetic disorders, cancer, and neurodegenerative diseases. For example, mutations in the BRCA1 and BRCA2 genes can increase the risk of breast and ovarian cancer, while mutations in the huntingtin gene can cause Huntington's disease. In some cases, mutant proteins can be targeted for therapeutic intervention. For example, drugs that inhibit the activity of mutant proteins or promote the degradation of mutant proteins may be used to treat certain types of cancer or other diseases.

Molecular chaperones are a class of proteins that assist in the folding, assembly, and transport of other proteins within cells. They play a crucial role in maintaining cellular homeostasis and preventing the accumulation of misfolded or aggregated proteins, which can lead to various diseases such as neurodegenerative disorders, cancer, and certain types of infections. Molecular chaperones function by binding to nascent or partially folded proteins, preventing them from aggregating and promoting their proper folding. They also assist in the assembly of multi-subunit proteins, such as enzymes and ion channels, by ensuring that the individual subunits are correctly folded and assembled into a functional complex. There are several types of molecular chaperones, including heat shock proteins (HSPs), chaperonins, and small heat shock proteins (sHSPs). HSPs are induced in response to cellular stress, such as heat shock or oxidative stress, and are involved in the refolding of misfolded proteins. Chaperonins, on the other hand, are found in the cytosol and the endoplasmic reticulum and are involved in the folding of large, complex proteins. sHSPs are found in the cytosol and are involved in the stabilization of unfolded proteins and preventing their aggregation. Overall, molecular chaperones play a critical role in maintaining protein homeostasis within cells and are an important target for the development of new therapeutic strategies for various diseases.

Trypsin is a proteolytic enzyme that is produced by the pancreas and is responsible for breaking down proteins into smaller peptides and amino acids. It is a serine protease that cleaves peptide bonds on the carboxyl side of lysine and arginine residues. Trypsin is an important digestive enzyme that helps to break down dietary proteins into smaller peptides and amino acids that can be absorbed and used by the body. It is also used in medical research and in the development of diagnostic tests and therapeutic agents.

Amino acids are organic compounds that are the building blocks of proteins. They are composed of an amino group (-NH2), a carboxyl group (-COOH), and a side chain (R group) that varies in size and structure. There are 20 different amino acids that are commonly found in proteins, each with a unique side chain that gives it distinct chemical and physical properties. In the medical field, amino acids are important for a variety of functions, including the synthesis of proteins, enzymes, and hormones. They are also involved in energy metabolism and the maintenance of healthy tissues. Deficiencies in certain amino acids can lead to a range of health problems, including muscle wasting, anemia, and neurological disorders. In some cases, amino acids may be prescribed as supplements to help treat these conditions or to support overall health and wellness.

In the medical field, ions are charged particles that are either positively or negatively charged. They are formed when an atom gains or loses electrons, and they play a crucial role in many bodily functions. For example, ions such as sodium, potassium, calcium, and chloride are essential for maintaining the proper balance of fluids in the body, which is necessary for proper nerve and muscle function. Imbalances in these ions can lead to a variety of medical conditions, such as hypertension, heart disease, and muscle cramps. In addition, ions are also important in the transmission of nerve impulses and the functioning of the immune system. They are also used in medical treatments such as electrotherapy and iontophoresis, which involve the application of electrical currents to the body to treat various conditions.

Hemeproteins are a class of proteins that contain a heme group, which is a complex of iron and porphyrin. Hemeproteins are found in many organisms and play important roles in a variety of biological processes, including oxygen transport, energy metabolism, and detoxification. The most well-known hemeprotein is hemoglobin, which is found in red blood cells and is responsible for carrying oxygen from the lungs to the body's tissues. Hemoglobin is composed of four subunits, each of which contains a heme group. The iron atom in the heme group can bind to oxygen molecules, allowing hemoglobin to transport oxygen throughout the body. Other examples of hemeproteins include myoglobin, which is found in muscle tissue and stores oxygen for use during periods of high physical activity, and cytochrome P450 enzymes, which are involved in the metabolism of drugs and other xenobiotics. Hemeproteins are important for many biological processes and are the subject of ongoing research in the medical field.

Adenosine triphosphate (ATP) is a molecule that serves as the primary energy currency in living cells. It is composed of three phosphate groups attached to a ribose sugar and an adenine base. In the medical field, ATP is essential for many cellular processes, including muscle contraction, nerve impulse transmission, and the synthesis of macromolecules such as proteins and nucleic acids. ATP is produced through cellular respiration, which involves the breakdown of glucose and other molecules to release energy that is stored in the bonds of ATP. Disruptions in ATP production or utilization can lead to a variety of medical conditions, including muscle weakness, fatigue, and neurological disorders. In addition, ATP is often used as a diagnostic tool in medical testing, as levels of ATP can be measured in various bodily fluids and tissues to assess cellular health and function.

Heme is a complex organic molecule that contains iron and is a vital component of hemoglobin, myoglobin, and other proteins involved in oxygen transport and storage in living organisms. It is also a component of various enzymes involved in metabolism and detoxification processes. In the medical field, heme is often used as a diagnostic tool to detect and monitor certain medical conditions, such as anemia (a deficiency of red blood cells or hemoglobin), liver disease (which can affect heme synthesis), and certain types of cancer (which can produce abnormal heme molecules). Heme is also used in the production of certain medications, such as heme-based oxygen carriers for use in patients with sickle cell disease or other conditions that affect oxygen transport. Additionally, heme is a component of some dietary supplements and is sometimes used to treat certain types of anemia.

Urea is a chemical compound that is produced in the liver as a waste product of protein metabolism. It is then transported to the kidneys, where it is filtered out of the blood and excreted in the urine. In the medical field, urea is often used as a diagnostic tool to measure kidney function. High levels of urea in the blood can be a sign of kidney disease or other medical conditions, while low levels may indicate malnutrition or other problems. Urea is also used as a source of nitrogen in fertilizers and as a raw material in the production of plastics and other chemicals.

Membrane proteins are proteins that are embedded within the lipid bilayer of a cell membrane. They play a crucial role in regulating the movement of substances across the membrane, as well as in cell signaling and communication. There are several types of membrane proteins, including integral membrane proteins, which span the entire membrane, and peripheral membrane proteins, which are only in contact with one or both sides of the membrane. Membrane proteins can be classified based on their function, such as transporters, receptors, channels, and enzymes. They are important for many physiological processes, including nutrient uptake, waste elimination, and cell growth and division.

Lysine is an essential amino acid that is required for the growth and maintenance of tissues in the human body. It is one of the nine essential amino acids that cannot be synthesized by the body and must be obtained through the diet. Lysine plays a crucial role in the production of proteins, including enzymes, hormones, and antibodies. It is also involved in the absorption of calcium and the production of niacin, a B vitamin that is important for energy metabolism and the prevention of pellagra. In the medical field, lysine is used to treat and prevent various conditions, including: 1. Herpes simplex virus (HSV): Lysine supplements have been shown to reduce the frequency and severity of outbreaks of HSV-1 and HSV-2, which cause cold sores and genital herpes, respectively. 2. Cold sores: Lysine supplements can help reduce the frequency and severity of cold sore outbreaks by inhibiting the replication of the herpes simplex virus. 3. Depression: Lysine has been shown to increase levels of serotonin, a neurotransmitter that regulates mood, in the brain. 4. Hair loss: Lysine is important for the production of hair, and deficiency in lysine has been linked to hair loss. 5. Wound healing: Lysine is involved in the production of collagen, a protein that is important for wound healing. Overall, lysine is an important nutrient that plays a crucial role in many aspects of human health and is used in the treatment and prevention of various medical conditions.

In the medical field, the term "Cytochrome c Group" refers to a family of heme-containing proteins that are involved in electron transfer reactions in the mitochondria of cells. These proteins play a crucial role in the electron transport chain, which is responsible for generating ATP, the energy currency of the cell. Cytochrome c is a small, water-soluble protein that is released from the mitochondria during apoptosis, a programmed cell death process. The release of cytochrome c from the mitochondria is a key event in the initiation of apoptosis, and it has been implicated in a number of diseases, including cancer, neurodegenerative disorders, and cardiovascular disease. Other members of the cytochrome c group include cytochrome b, cytochrome c1, and cytochrome oxidase. These proteins work together to transfer electrons from one molecule to another, ultimately leading to the reduction of oxygen to water. Any disruption in the function of these proteins can lead to a buildup of reactive oxygen species, which can damage cellular components and contribute to disease.

Recombinant fusion proteins are proteins that are produced by combining two or more genes in a single molecule. These proteins are typically created using genetic engineering techniques, such as recombinant DNA technology, to insert one or more genes into a host organism, such as bacteria or yeast, which then produces the fusion protein. Fusion proteins are often used in medical research and drug development because they can have unique properties that are not present in the individual proteins that make up the fusion. For example, a fusion protein might be designed to have increased stability, improved solubility, or enhanced targeting to specific cells or tissues. Recombinant fusion proteins have a wide range of applications in medicine, including as therapeutic agents, diagnostic tools, and research reagents. Some examples of recombinant fusion proteins used in medicine include antibodies, growth factors, and cytokines.

Aspartic acid is an amino acid that is naturally occurring in the human body. It is a non-essential amino acid, meaning that it can be synthesized by the body from other compounds and does not need to be obtained through the diet. Aspartic acid is found in high concentrations in the brain and spinal cord, and it plays a role in various physiological processes, including the production of neurotransmitters and the regulation of acid-base balance in the body. In the medical field, aspartic acid is sometimes used as a diagnostic tool to measure the function of the liver and kidneys, as well as to monitor the progression of certain diseases, such as cancer and HIV. It is also used as a dietary supplement in some cases.

Monoclonal antibodies (mAbs) are laboratory-made proteins that can mimic the immune system's ability to fight off harmful pathogens, such as viruses and bacteria. They are produced by genetically engineering cells to produce large quantities of a single type of antibody, which is specific to a particular antigen (a molecule that triggers an immune response). In the medical field, monoclonal antibodies are used to treat a variety of conditions, including cancer, autoimmune diseases, and infectious diseases. They can be administered intravenously, intramuscularly, or subcutaneously, depending on the condition being treated. Monoclonal antibodies work by binding to specific antigens on the surface of cells or pathogens, marking them for destruction by the immune system. They can also block the activity of specific molecules involved in disease processes, such as enzymes or receptors. Overall, monoclonal antibodies have revolutionized the treatment of many diseases, offering targeted and effective therapies with fewer side effects than traditional treatments.

Zinc is a chemical element that is essential for human health. In the medical field, zinc is used in a variety of ways, including as a supplement to treat and prevent certain health conditions. Zinc is involved in many important bodily functions, including immune system function, wound healing, and DNA synthesis. It is also important for the proper functioning of the senses of taste and smell. Zinc deficiency can lead to a range of health problems, including impaired immune function, delayed wound healing, and impaired growth and development in children. Zinc supplements are often recommended for people who are at risk of zinc deficiency, such as pregnant and breastfeeding women, people with certain medical conditions, and people who follow a vegetarian or vegan diet. In addition to its use as a supplement, zinc is also used in some medications, such as those used to treat acne and the common cold. It is also used in some over-the-counter products, such as antacids and nasal sprays. Overall, zinc is an important nutrient that plays a vital role in maintaining good health.

Serum Albumin, Bovine is a type of albumin, which is a type of protein found in the blood plasma of mammals. It is derived from the blood of cows and is used as a source of albumin for medical purposes. Albumin is an important protein in the body that helps to maintain the osmotic pressure of blood and transport various substances, such as hormones, drugs, and fatty acids, throughout the body. It is often used as a plasma expander in patients who have lost a significant amount of blood or as a replacement for albumin in patients with liver disease or other conditions that affect albumin production.

Hemoglobins are a group of proteins found in red blood cells (erythrocytes) that are responsible for carrying oxygen from the lungs to the body's tissues and carbon dioxide from the tissues back to the lungs. Hemoglobin is composed of four subunits, each of which contains a heme group that binds to oxygen. The oxygen binds to the iron atom in the heme group, allowing the hemoglobin to transport oxygen throughout the body. Hemoglobin also plays a role in regulating the pH of the blood and in the immune response. Abnormalities in hemoglobin can lead to various medical conditions, such as anemia, sickle cell disease, and thalassemia.

Calcium is a chemical element with the symbol Ca and atomic number 20. It is a vital mineral for the human body and is essential for many bodily functions, including bone health, muscle function, nerve transmission, and blood clotting. In the medical field, calcium is often used to diagnose and treat conditions related to calcium deficiency or excess. For example, low levels of calcium in the blood (hypocalcemia) can cause muscle cramps, numbness, and tingling, while high levels (hypercalcemia) can lead to kidney stones, bone loss, and other complications. Calcium supplements are often prescribed to people who are at risk of developing calcium deficiency, such as older adults, vegetarians, and people with certain medical conditions. However, it is important to note that excessive calcium intake can also be harmful, and it is important to follow recommended dosages and consult with a healthcare provider before taking any supplements.

In the medical field, carrier proteins are proteins that transport molecules across cell membranes or within cells. These proteins bind to specific molecules, such as hormones, nutrients, or waste products, and facilitate their movement across the membrane or within the cell. Carrier proteins play a crucial role in maintaining the proper balance of molecules within cells and between cells. They are involved in a wide range of physiological processes, including nutrient absorption, hormone regulation, and waste elimination. There are several types of carrier proteins, including facilitated diffusion carriers, active transport carriers, and ion channels. Each type of carrier protein has a specific function and mechanism of action. Understanding the role of carrier proteins in the body is important for diagnosing and treating various medical conditions, such as genetic disorders, metabolic disorders, and neurological disorders.

Plant proteins are proteins that are derived from plants. They are an important source of dietary protein for many people and are a key component of a healthy diet. Plant proteins are found in a wide variety of plant-based foods, including legumes, nuts, seeds, grains, and vegetables. They are an important source of essential amino acids, which are the building blocks of proteins and are necessary for the growth and repair of tissues in the body. Plant proteins are also a good source of fiber, vitamins, and minerals, and are generally lower in saturated fat and cholesterol than animal-based proteins. In the medical field, plant proteins are often recommended as part of a healthy diet for people with certain medical conditions, such as heart disease, diabetes, and high blood pressure.

Polydeoxyribonucleotides, also known as poly(dNTPs), are polymers of deoxyribonucleotides, which are the building blocks of DNA. They are composed of a sugar molecule (deoxyribose), a phosphate group, and a nitrogenous base (adenine, thymine, cytosine, or guanine). In the medical field, poly(dNTPs) are commonly used as a substrate in DNA polymerase reactions, which are essential for DNA replication and repair. They are also used in various molecular biology techniques, such as polymerase chain reaction (PCR), DNA sequencing, and DNA synthesis. Poly(dNTPs) are available in different concentrations and purities, and their selection depends on the specific application and experimental requirements.

In the medical field, "iron" refers to a mineral that is essential for the production of red blood cells, which carry oxygen throughout the body. Iron is also important for the proper functioning of the immune system, metabolism, and energy production. Iron deficiency is a common condition that can lead to anemia, a condition in which the body does not have enough red blood cells to carry oxygen to the body's tissues. Symptoms of iron deficiency anemia may include fatigue, weakness, shortness of breath, and pale skin. Iron supplements are often prescribed to treat iron deficiency anemia, and dietary changes may also be recommended to increase iron intake. However, it is important to note that excessive iron intake can also be harmful, so it is important to follow the recommended dosage and consult with a healthcare provider before taking any iron supplements.

Saccharomyces cerevisiae proteins are proteins that are produced by the yeast species Saccharomyces cerevisiae. This yeast is commonly used in the production of bread, beer, and wine, as well as in scientific research. In the medical field, S. cerevisiae proteins have been studied for their potential use in the treatment of various diseases, including cancer, diabetes, and neurodegenerative disorders. Some S. cerevisiae proteins have also been shown to have anti-inflammatory and immunomodulatory effects, making them of interest for the development of new therapies.

In the medical field, disulfides refer to chemical compounds that contain two sulfur atoms connected by a single bond. Disulfides are commonly found in proteins, where they play an important role in maintaining the structure and function of the protein. One of the most well-known examples of a disulfide is the cystine molecule, which is composed of two cysteine amino acids that are linked together by a disulfide bond. Disulfide bonds are important for the proper folding and stability of proteins, and they can also play a role in the function of the protein. Disulfides can also be found in other types of molecules, such as lipids and carbohydrates. In these cases, disulfides may play a role in the structure and function of the molecule, or they may be involved in signaling pathways within the body. Overall, disulfides are an important class of chemical compounds that play a variety of roles in the body, including the maintenance of protein structure and function, and the regulation of signaling pathways.

Trifluoroethanol, also known as 2,2,2-trifluoroethanol or TFE, is a colorless, volatile liquid with a sweet odor. It is a polar solvent that is commonly used in the medical field as a chemical reagent and a solvent for various organic compounds. In the medical field, trifluoroethanol is used in a variety of applications, including as a solvent for the extraction of proteins and other biological molecules, as a denaturant for proteins, and as a stabilizer for enzymes. It is also used as a solvent for the purification of certain drugs and as a component in the production of certain pharmaceuticals. Trifluoroethanol is generally considered to be safe for use in the medical field, although it can be toxic in high concentrations. It is important to handle it with care and to follow proper safety procedures when working with this chemical.

Magnesium is a mineral that is essential for many bodily functions. It is involved in over 300 enzymatic reactions in the body, including the production of energy, the synthesis of proteins and DNA, and the regulation of muscle and nerve function. In the medical field, magnesium is used to treat a variety of conditions, including: 1. Hypomagnesemia: A deficiency of magnesium in the blood. This can cause symptoms such as muscle cramps, spasms, and seizures. 2. Cardiac arrhythmias: Abnormal heart rhythms that can be caused by low levels of magnesium. 3. Pre-eclampsia: A condition that can occur during pregnancy and is characterized by high blood pressure and protein in the urine. Magnesium supplementation may be used to treat this condition. 4. Chronic kidney disease: Magnesium is often lost in the urine of people with chronic kidney disease, and supplementation may be necessary to maintain adequate levels. 5. Alcohol withdrawal: Magnesium supplementation may be used to treat symptoms of alcohol withdrawal, such as tremors and seizures. 6. Muscle spasms: Magnesium can help to relax muscles and relieve spasms. 7. Anxiety and depression: Some studies have suggested that magnesium supplementation may help to reduce symptoms of anxiety and depression. Magnesium is available in various forms, including oral tablets, capsules, and intravenous solutions. It is important to note that high levels of magnesium can also be toxic, so it is important to use magnesium supplements under the guidance of a healthcare provider.

Escherichia coli (E. coli) is a type of bacteria that is commonly found in the human gut. E. coli proteins are proteins that are produced by E. coli bacteria. These proteins can have a variety of functions, including helping the bacteria to survive and thrive in the gut, as well as potentially causing illness in humans. In the medical field, E. coli proteins are often studied as potential targets for the development of new treatments for bacterial infections. For example, some E. coli proteins are involved in the bacteria's ability to produce toxins that can cause illness in humans, and researchers are working to develop drugs that can block the activity of these proteins in order to prevent or treat E. coli infections. E. coli proteins are also used in research to study the biology of the bacteria and to understand how it interacts with the human body. For example, researchers may use E. coli proteins as markers to track the growth and spread of the bacteria in the gut, or they may use them to study the mechanisms by which the bacteria causes illness. Overall, E. coli proteins are an important area of study in the medical field, as they can provide valuable insights into the biology of this important bacterium and may have potential applications in the treatment of bacterial infections.

In the medical field, lipid bilayers refer to the two layers of phospholipid molecules that form the basic structure of cell membranes. The lipid bilayer is composed of a hydrophilic (water-loving) head and a hydrophobic (water-fearing) tail. The hydrophilic heads face outward, towards the aqueous environment of the cell, while the hydrophobic tails face inward, towards each other. This arrangement creates a barrier that separates the inside of the cell from the outside environment, while also allowing for the selective passage of molecules in and out of the cell. The lipid bilayer is essential for maintaining the integrity and function of cells, and is involved in a wide range of cellular processes, including cell signaling, metabolism, and transport.

Oligodeoxyribonucleotides (ODNs) are short chains of DNA or RNA that are synthesized in the laboratory. They are typically used as tools in molecular biology research, as well as in therapeutic applications such as gene therapy. ODNs can be designed to bind to specific DNA or RNA sequences, and can be used to modulate gene expression or to introduce genetic changes into cells. They can also be used as primers in PCR (polymerase chain reaction) to amplify specific DNA sequences. In the medical field, ODNs are being studied for their potential use in treating a variety of diseases, including cancer, viral infections, and genetic disorders. For example, ODNs can be used to silence specific genes that are involved in disease progression, or to stimulate the immune system to attack cancer cells.

Proline is an amino acid that is commonly found in proteins. It is a non-essential amino acid, meaning that it can be synthesized by the body from other amino acids. In the medical field, proline is often used as a diagnostic tool to measure the levels of certain enzymes in the body, such as alanine transaminase (ALT) and aspartate transaminase (AST). These enzymes are released into the bloodstream when the liver is damaged, so elevated levels of proline can indicate liver disease. Proline is also used in the treatment of certain medical conditions, such as Peyronie's disease, which is a condition that causes curvature of the penis. Proline has been shown to help improve the flexibility of the penis and reduce the curvature associated with Peyronie's disease.

In the medical field, oligopeptides are short chains of amino acids that typically contain between two and 50 amino acids. They are often used in various medical applications due to their unique properties and potential therapeutic effects. One of the main benefits of oligopeptides is their ability to penetrate the skin and reach underlying tissues, making them useful in the development of topical treatments for a variety of conditions. For example, oligopeptides have been shown to improve skin elasticity, reduce the appearance of wrinkles, and promote the growth of new skin cells. Oligopeptides are also used in the development of medications for a variety of conditions, including osteoporosis, diabetes, and hypertension. They work by interacting with specific receptors in the body, which can help to regulate various physiological processes and improve overall health. Overall, oligopeptides are a promising area of research in the medical field, with potential applications in a wide range of therapeutic areas.

Micelles are small, spherical structures that form when surfactant molecules, such as phospholipids, are dissolved in water. In the medical field, micelles are often used as drug delivery systems to transport drugs across cell membranes and into cells. This is because the hydrophobic core of the micelle can encapsulate hydrophobic drugs, while the hydrophilic shell of the micelle can interact with water and other polar molecules. This allows the drug to be transported through the bloodstream and into cells, where it can be released and exert its therapeutic effect. Micelles are also used in various medical imaging techniques, such as magnetic resonance imaging (MRI), to enhance the contrast between different tissues in the body.

In the medical field, nucleotides are the building blocks of nucleic acids, which are the genetic material of cells. Nucleotides are composed of three components: a nitrogenous base, a pentose sugar, and a phosphate group. There are four nitrogenous bases in DNA: adenine (A), thymine (T), cytosine (C), and guanine (G). There are also four nitrogenous bases in RNA: adenine (A), uracil (U), cytosine (C), and guanine (G). The sequence of these nitrogenous bases determines the genetic information encoded in DNA and RNA.

Alanine is an amino acid that is a building block of proteins. It is an essential amino acid, meaning that it cannot be synthesized by the body and must be obtained through the diet. Alanine plays a number of important roles in the body, including: 1. Energy production: Alanine can be converted into glucose, which is a source of energy for the body. 2. Muscle function: Alanine is involved in the metabolism of muscle tissue and can help to prevent muscle damage. 3. Liver function: Alanine is an important component of the liver's detoxification process and can help to protect the liver from damage. 4. Acid-base balance: Alanine helps to regulate the body's acid-base balance by buffering excess acid in the blood. In the medical field, alanine is often used as a biomarker to assess liver function. Elevated levels of alanine in the blood can indicate liver damage or disease. Alanine is also used as a dietary supplement to support muscle growth and recovery.

RNA, or ribonucleic acid, is a type of nucleic acid that is involved in the process of protein synthesis in cells. It is composed of a chain of nucleotides, which are made up of a sugar molecule, a phosphate group, and a nitrogenous base. There are three types of RNA: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). In the medical field, RNA is often studied as a potential target for the development of new drugs and therapies. For example, some researchers are exploring the use of RNA interference (RNAi) to silence specific genes and treat diseases such as cancer and viral infections. Additionally, RNA is being studied as a potential biomarker for various diseases, as changes in the levels or structure of certain RNA molecules can indicate the presence of a particular condition.

Histidine is an amino acid that is naturally occurring in the human body. It is a building block of proteins and is essential for the proper functioning of many bodily processes. In the medical field, histidine is often used as a diagnostic tool to help diagnose certain medical conditions. For example, high levels of histidine in the blood can be a sign of a genetic disorder called histidinemia, which can cause a range of symptoms including intellectual disability, seizures, and liver problems. Histidine is also used in the treatment of certain medical conditions, such as acidosis, which is a condition in which the body's pH balance is disrupted.

Adenosine diphosphate (ADP) is a molecule that plays a crucial role in various metabolic processes in the body, particularly in the regulation of energy metabolism. It is a nucleotide that is composed of adenine, ribose, and two phosphate groups. In the medical field, ADP is often used as a diagnostic tool to assess the function of platelets, which are blood cells that play a critical role in blood clotting. ADP is a potent activator of platelets, and a decrease in platelet aggregation in response to ADP is often an indication of a bleeding disorder. ADP is also used in the treatment of various medical conditions, including heart disease, stroke, and migraines. For example, drugs that inhibit ADP receptors on platelets, such as clopidogrel and ticagrelor, are commonly used to prevent blood clots in patients with heart disease or stroke. Overall, ADP is a critical molecule in the regulation of energy metabolism and the function of platelets, and its role in the medical field is significant.

In the medical field, a protein subunit refers to a smaller, functional unit of a larger protein complex. Proteins are made up of chains of amino acids, and these chains can fold into complex three-dimensional structures that perform a wide range of functions in the body. Protein subunits are often formed when two or more protein chains come together to form a larger complex. These subunits can be identical or different, and they can interact with each other in various ways to perform specific functions. For example, the protein hemoglobin, which carries oxygen in red blood cells, is made up of four subunits: two alpha chains and two beta chains. Each of these subunits has a specific structure and function, and they work together to form a functional hemoglobin molecule. In the medical field, understanding the structure and function of protein subunits is important for developing treatments for a wide range of diseases and conditions, including cancer, neurological disorders, and infectious diseases.

Gramicidin is a type of antibiotic that is derived from a soil bacterium called Bacillus brevis. It is a polypeptide antibiotic that is effective against a wide range of gram-positive bacteria, including Staphylococcus aureus, Streptococcus pyogenes, and Bacillus anthracis. Gramicidin works by disrupting the cell membrane of bacteria, causing it to leak and eventually leading to cell death. It is often used topically to treat skin infections, such as impetigo and cellulitis, and is also used to treat certain types of pneumonia and meningitis. However, gramicidin is not effective against gram-negative bacteria and can cause side effects such as allergic reactions and kidney damage when used in high doses.

Adenosine triphosphatases (ATPases) are a group of enzymes that hydrolyze adenosine triphosphate (ATP) to adenosine diphosphate (ADP) and inorganic phosphate (Pi). These enzymes play a crucial role in many cellular processes, including energy production, muscle contraction, and ion transport. In the medical field, ATPases are often studied in relation to various diseases and conditions. For example, mutations in certain ATPase genes have been linked to inherited disorders such as myopathy and neurodegenerative diseases. Additionally, ATPases are often targeted by drugs used to treat conditions such as heart failure, cancer, and autoimmune diseases. Overall, ATPases are essential enzymes that play a critical role in many cellular processes, and their dysfunction can have significant implications for human health.

DNA primers are short, single-stranded DNA molecules that are used in a variety of molecular biology techniques, including polymerase chain reaction (PCR) and DNA sequencing. They are designed to bind to specific regions of a DNA molecule, and are used to initiate the synthesis of new DNA strands. In PCR, DNA primers are used to amplify specific regions of DNA by providing a starting point for the polymerase enzyme to begin synthesizing new DNA strands. The primers are complementary to the target DNA sequence, and are added to the reaction mixture along with the DNA template, nucleotides, and polymerase enzyme. The polymerase enzyme uses the primers as a template to synthesize new DNA strands, which are then extended by the addition of more nucleotides. This process is repeated multiple times, resulting in the amplification of the target DNA sequence. DNA primers are also used in DNA sequencing to identify the order of nucleotides in a DNA molecule. In this application, the primers are designed to bind to specific regions of the DNA molecule, and are used to initiate the synthesis of short DNA fragments. The fragments are then sequenced using a variety of techniques, such as Sanger sequencing or next-generation sequencing. Overall, DNA primers are an important tool in molecular biology, and are used in a wide range of applications to study and manipulate DNA.

In the medical field, "DNA, Superhelical" refers to a type of DNA molecule that has a twisted or coiled structure, known as a double helix. The double helix is composed of two strands of nucleotides that are held together by hydrogen bonds between the nitrogenous bases. Superhelical DNA is characterized by an additional level of twist or winding around its axis, which is known as supercoiling. This supercoiling can occur in either a left-handed or right-handed direction, and it is thought to play a role in regulating gene expression and other cellular processes. Supercoiling can be induced by a variety of factors, including changes in temperature, pH, or the presence of certain enzymes. It can also be influenced by the presence of proteins that bind to the DNA and help to stabilize the superhelical structure. In medical research, supercoiled DNA is often used as a model system for studying the behavior of DNA under different conditions, as well as for developing new techniques for manipulating and analyzing DNA. It is also an important component of many genetic engineering and biotechnology applications.

Chromatin is a complex of DNA, RNA, and proteins that makes up the chromosomes in the nucleus of a cell. It plays a crucial role in regulating gene expression and maintaining the structure of the genome. In the medical field, chromatin is studied in relation to various diseases, including cancer, genetic disorders, and neurological conditions. For example, chromatin remodeling is a process that can alter the structure of chromatin and affect gene expression, and it has been implicated in the development of certain types of cancer. Additionally, chromatin-based therapies are being explored as potential treatments for diseases such as Alzheimer's and Parkinson's.

In the medical field, "Poly dA-dT" refers to a type of DNA polymer that is composed of alternating adenine (A) and thymine (T) nucleotides. This type of DNA is often used in laboratory experiments as a model system for studying DNA replication and repair mechanisms, as well as for developing new DNA-based technologies such as gene therapy and DNA sequencing. Poly dA-dT DNA is also known to form stable double-stranded structures that are resistant to degradation by nucleases, making it useful for a variety of applications in molecular biology and biotechnology.

Phenylalanine is an essential amino acid that is required for the production of proteins in the body. It is one of the building blocks of the protein called tyrosine, which is important for the production of hormones, neurotransmitters, and other important molecules in the body. Phenylalanine is also used in the production of certain neurotransmitters, including dopamine and norepinephrine, which play important roles in regulating mood, motivation, and other aspects of brain function. In the medical field, phenylalanine is often used as a dietary supplement to help individuals with certain medical conditions, such as phenylketonuria (PKU), which is a genetic disorder that affects the metabolism of phenylalanine. In PKU, the body is unable to properly break down phenylalanine, which can lead to a buildup of the amino acid in the blood and brain, causing damage to the brain and other organs. Phenylalanine is also used in some medications, such as certain antidepressants, to help regulate the production of neurotransmitters in the brain. However, it is important to note that phenylalanine can interact with other medications and may not be safe for everyone to take, so it is important to consult with a healthcare provider before taking any supplements or medications containing phenylalanine.

Adenylyl imidodiphosphate, also known as AMP-PPi or AMP-P2, is a molecule that plays a role in various cellular processes, including energy metabolism and signal transduction. It is a product of the reaction between adenosine monophosphate (AMP) and inorganic pyrophosphate (PPi), and is involved in the regulation of enzymes that catalyze the synthesis and breakdown of high-energy molecules such as ATP. In the medical field, AMP-PPi is sometimes used as a diagnostic tool to measure the activity of certain enzymes, and it has also been studied as a potential therapeutic target for the treatment of various diseases, including cancer and neurodegenerative disorders.

In the medical field, "salts" typically refers to compounds that contain ions of metals or other elements combined with non-metallic elements such as chlorine, sulfur, or phosphorus. These compounds are often used in various medical applications, including: 1. Electrolyte balance: Salts are essential for maintaining the balance of electrolytes in the body. Electrolytes are minerals that carry an electric charge and are necessary for many bodily functions, including muscle and nerve function, hydration, and acid-base balance. 2. Medications: Salts are often used as active ingredients in medications. For example, sodium chloride (table salt) is used as an ingredient in many over-the-counter pain relievers and cold medicines. 3. Antiseptics: Salts such as silver sulfadiazine are used as antiseptics to prevent infection in wounds. 4. Diuretics: Salts such as potassium chloride are used as diuretics to increase urine production and help remove excess fluids from the body. 5. Supplements: Salts such as magnesium sulfate are used as supplements to provide essential minerals that may be lacking in the diet. Overall, salts play an important role in many medical applications and are essential for maintaining proper bodily function.

Glycine is an amino acid that is essential for the proper functioning of the human body. It is a non-essential amino acid, meaning that the body can synthesize it from other compounds, but it is still important for various physiological processes. In the medical field, glycine is used as a dietary supplement to support muscle growth and recovery, as well as to improve sleep quality. It is also used in the treatment of certain medical conditions, such as liver disease, as it can help to reduce the buildup of toxins in the liver. Glycine is also used in the production of various medications, including antibiotics and tranquilizers. It has been shown to have a calming effect on the nervous system and may be used to treat anxiety and other mental health conditions. Overall, glycine is an important nutrient that plays a vital role in many physiological processes in the body.

List of protein structure prediction software Chou PY, Fasman GD (1974). "Prediction of protein conformation". Biochemistry. 13 ... Chou PY, Fasman GD (1978). "Empirical predictions of protein conformation". Annu Rev Biochem. 47: 251-276. doi:10.1146/annurev. ... doi:10.1093/protein/11.5.345. PMID 9681866. Chen H, Gu F, Huang Z (2006). "Improved Chou-Fasman method for protein secondary ... Kyngas J, Valjakka J (1998). "Unreliability of the Chou-Fasman parameters in predicting protein secondary structure". Protein ...
"Improved prediction of protein side-chain conformations with SCWRL4". Proteins. 77 (4): 778-95. doi:10.1002/prot.22488. PMC ... Biology portal Protein design Protein function prediction Protein-protein interaction prediction Gene prediction Protein ... This same cutoff is still used by the Protein Information Resource (PIR). A protein family comprises proteins with the same ... Proteins are chains of amino acids joined together by peptide bonds. Many conformations of this chain are possible due to the ...
... is the local spatial conformation of the polypeptide backbone excluding the side chains. The two ... The original beta-sheet conformation article.) Pauling L, Corey RB, Branson HR (1951). "The structure of proteins; two hydrogen ... Amino acids that prefer to adopt helical conformations in proteins include methionine, alanine, leucine, glutamate and lysine ... Chou PY, Fasman GD (1978). "Empirical predictions of protein conformation". Annual Review of Biochemistry. 47: 251-76. doi: ...
Chou, Peter Y.; Fasman, Gerald D. (1974-01-15). "Prediction of protein conformation". Biochemistry. 13 (2): 222-245. doi: ... UPF0575 protein C19orf67 is a protein which in humans (Homo sapiens) is encoded by the C19orf67 gene. Orthologs of C19orf67 are ... Protein Engineering, Design and Selection. 20 (11): 561-567. doi:10.1093/protein/gzm057. ISSN 1741-0126. PMID 17993650. " ... The protein is expressed at low levels throughout the body with the exception of the testis and breast tissue. Where it is ...
Chou, Peter Y.; Fasman, Gerald D. (1974-01-15). "Prediction of protein conformation". Biochemistry. 13 (2): 222-245. doi: ... "Protein BLAST: search protein databases using a protein query". blast.ncbi.nlm.nih.gov. Retrieved 2018-05-04. EMBL-EBI. " ... "uncharacterized protein C21orf58 isoform 1 [Homo sapiens] - Protein - NCBI". ncbi.nlm.nih.gov. Retrieved 2018-02-04. "C21orf58 ... "KLHL20 - Kelch-like protein 20 - Homo sapiens (Human) - KLHL20 gene & protein". uniprot.org. Retrieved 2018-05-06. "TimeTree ...
Ramachandran, G.N.; Sasiskharan, V. (1968). Conformation of polypeptides and proteins. Advances in Protein Chemistry. Vol. 23. ... Hovmöller, S.; Zhou, T.; Ohlson, T. (2002). "Conformations of amino acids in proteins". Acta Crystallographica D. 58 (Pt 5): ... Chakrabarti, Pinak; Pal, Debnath (2001). "The interrelationships of side-chain and main-chain conformations in proteins". ... Richardson, J.S. (1981). "The Anatomy and Taxonomy of Protein Structure". Anatomy and Taxonomy of Protein Structures. Advances ...
"Conformation of polypeptides and proteins". Advances in Protein Chemistry Volume 23. Advances in Protein Chemistry. Vol. 23. pp ... such as protein-protein interactions (PPI), protein-peptide interactions, protein-ligand interactions (PLI), and protein-DNA ... ProtCID: The Protein Common Interface Database Database of similar protein-protein interfaces in crystal structures of ... protein threading, de novo protein structure prediction, and secondary structure prediction is available in the list of protein ...
Ramachandran, G. N.; Sasisekharan, V. (1968). "Conformation of polypeptides and proteins". Advances in Protein Chemistry. 23: ... While the majority of the Peptide bonds within proteins exist in trans (planar) conformation because of the partial double-bond ... step in the process of protein folding. Immunophilins, with their prolyl isomerase activity, thus function as protein-folding ... FK506 binds with high affinity to other smaller proteins, such as FKBP-12. FKBP-12 and cyclophilins both share common peptide- ...
... publications indexed by Google Scholar Sternberg, Michael Joseph Ezra (1977). Studies of protein conformation ... Sternberg's research interests are in protein structure prediction, protein function prediction, prediction of macromolecular ... Protein Engineering: a practical approach and Protein Structure Prediction: a practical approach. During his DPhil research at ... Zvelebil, M. J.; Barton, G. J.; Taylor, W. R.; Sternberg, M. J. (1987). "Prediction of protein secondary structure and active ...
Celada, F.; Schumaker, V.N.; Sercarz, E.E. (2012). Protein Conformation as an Immunological Signal. Springer US. p. 240. ISBN ...
Damberger FF, Christen B, Pérez DR, Hornemann S, Wüthrich K (October 2011). "Cellular prion protein conformation and function ... in the prion protein. Others insert additional amino acids into the protein or cause an abnormally short protein to be made. ... These mutations cause the cell to make prion proteins with an abnormal structure. The abnormal protein PrPSc accumulates in the ... Specific sites along the protein bind other proteins, biomolecules, and metals. These interfaces allow specific sets of cells ...
Levitt, M. (1976). "A simplified representation of protein conformations for rapid simulation of protein folding". Journal of ... Michael Levitt publications indexed by Google Scholar Levitt, Michael (1972). Conformation analysis of proteins (PhD thesis). ... He has also worked on simplified representations of protein structure for analysing folding and packing, as well as developing ... Xia, Y.; Huang, E. S.; Levitt, M.; Samudrala, R. (2000). "Ab initio construction of protein tertiary structures using a ...
Sternberg, Michael Joseph Ezra (1977). Studies of protein conformation (DPhil thesis). University of Oxford. Phillips, D. C.; ...
Sibanda, BL; Blundell TL; Thornton JM (1989). "Conformation of β-hairpins in protein structures. A systematic classification ... Leader, DP; Milner-White EJ (2009). "Motivated Proteins: A web application for studying small three-dimensional protein motifs ... Chan, EAW; Hutchinson EG (1993). "Identification, classification and analysis of β-bulges in proteins". Protein Science. 2 (10 ... Two websites are available for finding and examining β bulge loops in proteins, Motivated Proteins: [1] and PDBeMotif: [2]. ...
Sibanda, B. L.; Blundell, T. L.; Thornton, J. M. (1989). "Conformation of beta-hairpins in protein structures. A systematic ... Thornton, J. M.; Singh, J; Campbell, S; Blundell, T. L. (1988). "Protein-protein recognition via side-chain interactions". ... "The Protein Feature Ontology: A tool for the unification of protein feature annotations". Bioinformatics. 24 (23): 2767-2772. ... for evaluating the quality of experimentally defined protein structures: this is used widely to check protein structures. She ...
"Roles of electrostatics and conformation in protein-crystal interactions". PLOS ONE. 5 (2): e9330. Bibcode:2010PLoSO...5.9330A ... Protein pages needing a picture, Glycoproteins, Extracellular matrix proteins, Matricellular proteins). ... OPN belongs to a family of secreted acidic proteins (SIBLINGs, Small Integrin Binding LIgand N-Glycosylated proteins) whose ... "Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin". Biochemistry. 52 (31): ...
Glycolipid transfer protein is a protein that in humans is encoded by the GLTP gene. The protein encoded by this gene is ... probing conformation using fluorescence spectroscopy". Biochemistry. 43 (31): 10285-94. doi:10.1021/bi0495432. PMC 2593833. ... "Entrez Gene: GLTP glycolipid transfer protein". Brown RE, Mattjus P (2007). "Glycolipid transfer proteins". Biochim. Biophys. ... 2004). "Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on ...
During illumination with light, these proteins change their conformation. In the process they gain or lose their ability to ... Some fluorescent proteins can be switched on and off by light of an appropriate wavelength. They can be used in a RESOLFT-type ... Just as with proteins, also some organic dyes can change their structure upon illumination. The ability to fluoresce of such ... Inducing conformational changes in proteins can be achieved already at much lower switching light intensities as compared to ...
Janin, J.; Wodak, S. (1978). "Conformation of amino acid side-chains in proteins*1". Journal of Molecular Biology. 125 (3): 357 ... In biochemistry, a Janin plot, like a Ramachandran plot, is a way to visualize dihedral angle distributions in protein ...
Durussel I, Rhyner JA, Strehler EE, Cox JA (1993). "Cation binding and conformation of human calmodulin-like protein". ... Calmodulin-like protein 3 is a protein that in humans is encoded by the CALML3 gene. GRCh38: Ensembl release 89: ... Rogers MS, Kobayashi T, Pittelkow MR, Strehler EE (2001). "Human calmodulin-like protein is an epithelial-specific protein ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. Bibcode: ...
Sibanda, B.L.; Blundell, T.L.; Thornton, J.M. (1989). "Conformation of β-hairpins in protein structures:: A systematic ... Bu Z, Callaway DJ (2011). "Proteins move! Protein dynamics and long-range allostery in cell signaling". Protein Structure and ... 1968). "Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units". ... Rajashankar KR, Ramakumar S (1996). "Pi-turns in proteins and peptides: Classification, conformation, occurrence, hydration and ...
Method of modifying the conformation of food and feed proteins. US Patent. G Szabolcsi, 1991. Enzimes Analizis. Akadémiai Kiadó ...
The conformation of a receptor protein composes the functional state. Ligands include substrates, inhibitors, activators, ... are frequent in protein complexes, and are ligands that bind more than one protein chain, typically in or near protein ... The binding typically results in a change of conformational isomerism (conformation) of the target protein. In DNA-ligand ... Ligand binding to a receptor protein alters the conformation by affecting the three-dimensional shape orientation. ...
"Lysine Acetylation Controls Local Protein Conformation by Influencing Proline Isomerization". Molecular Cell. 55 (5): 733-744. ... a process that can lock proteins in a nonnative structure that can affect render the protein temporarily ineffective. Although ... Without the cis conformation of the pSer5-Pro6 bond, created by Ess1/Pin1, Nrd1 cannot bind to RNAP II. Any variation from this ... The protein p53, along with p63 and p73, are responsible for ensuring that alterations to the genome are corrected and for ...
43 (4) 482-487 (1998) ^ "Toy Model Studies of Soliton Mediated Protein Folding and Conformation Changes" Caspi, S., Ben-Jacob, ... 47, 522-527 (1999). ^ "Conformation changes and folding of proteins mediated by Davidov's soliton". Caspi, S., Ben-Jacob, E., ... Soliton-mediated protein folding.[20][21][22] Pattern formation and self-organization.[23][24][25][26][27][28][29][30][31] In ... "Lethal protein produced in response to competition between sibling bacterial colonies". Be'er, A., Ariel, G., Kalishman, O., ...
Predictions of Protein Structure and the Principles of Protein Conformation. New York: Plenum Press. pp. 599-623. ISBN 978-0- ... These properties influence protein structure and protein-protein interactions. The water-soluble proteins tend to have their ... The protein is broken down into amino acids in the process of digestion. They are then used to synthesize new proteins, other ... Suchanek M, Radzikowska A, Thiele C (April 2005). "Photo-leucine and photo-methionine allow identification of protein-protein ...
"Ubiquitin chain conformation regulates recognition and activity of interacting proteins". Nature. 492 (7428): 266-70. Bibcode: ... "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957-68. doi:10.1016/j.cell ... Polyubiquitin-C is a protein encoded by the UBC gene in humans. Polyubiquitin-C is one of the sources of ubiquitin, along with ... Chen L, Dong W, Zou T, Ouyang L, He G, Liu Y, Qi Y (August 2008). "Protein phosphatase 4 negatively regulates LPS cascade by ...
Prediction of Protein Structures and the Principles of Protein Conformation. New York: Plenum. pp. 599-623. ISBN 978-0-306- ... Alanine (symbol Ala or A), or α-alanine, is an α-amino acid that is used in the biosynthesis of proteins. It contains an amine ... It is a catabolic pathway, and relies upon protein breakdown in the muscle tissue. Whether and to what extent it occurs in non- ... In this model the selection of monomers (i.e. amino acids) for ribosomal protein synthesis is rather limited to those Alanine ...
β-Sheets predominate as the secondary level of protein conformation.[citation needed] The structure of trans-sialidase includes ... There are two major proteins on the surface of influenza virus particles. One is the lectin haemagglutinin protein with three ... The first step involves the distortion of the α-sialoside from a 2C5 chair conformation (the lowest-energy form in solution) to ... Protein pages needing a picture, Genes on human chromosome 6, Genes on human chromosome 2, Genes on human chromosome 11, ...
Sibanda, B.L.; Blundell, T.L.; Thorton, J.M. (1985). "Conformations of Beta-Hairpins in Protein Structures". Nature(London) 316 ... To see this clearly, the Pin1 Domain protein is shown to the left as an example. Proteins that are β-sheet rich, also called WW ... function by adhering to proline-rich and/or phosphorylated peptides to mediate protein-protein interactions. The "WW" refers to ... have used protein NMR to show that beta-hairpins can be formed from isolated short peptides in aqueous solution, suggesting ...
All species are found to have a restricting influence on the conformation of a peptide bond. Nonplanar deformations of the ... various hydrogen bonding species that are similar to those typically found in the environment of a peptide within a protein ... Theoretical Studies of Environmental Effects on Protein Conformation: Flexibility of the Peptide Bond S. Scheiner and C. W. ... Theoretical Studies of Environmental Effects on Protein Conformation. 1. Flexibility of the Peptide Bond ...
Kang HE, Weng CC, Saijo E, Saylor V, Bian J, Kim S, et al. Characterization of conformation-dependent prion protein epitopes. J ... Telling GC, Parchi P, DeArmond SJ, Cortelli P, Montagna P, Gabizon R, et al. Evidence for the conformation of the pathologic ... Angers RC, Kang HE, Napier D, Browning S, Seward T, Mathiason C, et al. Prion strain mutation determined by prion protein ... Peretz D, Williamson RA, Legname G, Matsunaga Y, Vergara J, Burton DR, et al. A change in the conformation of prions ...
Cooperative Unfolding of Compact Conformations of the Intrinsically Disordered Protein Osteopontin ... Cooperative Unfolding of Compact Conformations of the Intrinsically Disordered Protein Osteopontin Kurzbach, D., Platzer, G., ... Cooperative Unfolding of Compact Conformations of the Intrinsically Disordered Protein Osteopontin. Biochemistry, 52(31), 5167- ...
human Neurotensin Receptor 1 (hNTSR1) - Gi1 Protein Complex in canonical conformation (C state). Help ...
Protein Binding * Protein Conformation * Protein Interaction Domains and Motifs Substances * DNA-Binding Proteins ...
The TRIP13 gene provides instructions for making a protein that has several roles in cell division. Learn about this gene and ... TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching. Elife. 2015 Apr 28;4:e07367. doi: ... As a result, cells lack TRIP13 protein. A shortage of this protein impairs the spindle assembly checkpoint, and cell division ... The TRIP13 gene provides instructions for making a protein that has several roles in cell division. One important role is to ...
... a flexible engine to explore backbone conformations and their relationships to covalent geometry. ... Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry. ...
The B.1.1.7 variant carries a mutation in the S protein (N501Y) that affects the conformation of receptor-binding domain. This ... Abbreviations: del = deletion; E = envelope protein; N = nucleocapsid protein; ORF = open reading frame; S = spike protein. ... Characteristic mutations (protein: mutation). No. of current sequence-confirmed cases. No. of countries with sequences. ... Early in the pandemic, variants of SARS-CoV-2 containing the D614G mutation in the spike (S) protein that increases receptor ...
These proteins protect ribosomes by binding them and changing their shape or conformation. The change in the ribosome shape ... Ribosomal protection proteins (RPP) are another source of resistance bacteria use to protect themselves from antibiotics. ... Role of ribosomal protein S12 in peptide chain elongation: analysis of pleiotropic, streptomycin-resistant mutants of ... Antibiotic resistance in bacteria can also be achieved when mutations in a ribosome or protein change the site where an ...
Provides horses with necessary dietary sulfur which helps in the proper conformation of proteins associated with connective ...
The antimicrobial functionality of LF is dependent on its protein conformation and milieu conditions (Naidu and Arnold, 1997). ... LF is considered a milk protein (provision 79/112/EEC allows all types of milk protein to be labeled as milk protein) and hence ... The EU has a directive 83/417/EEC for the use of protein derived from milk, but LF could be included in this directive when it ... Lactoferrin-binding proteins in Shigella flexneri. Infect. Immun. 60: 2619-2626.. Tomita, M., Takase, M., Wakabayashi, H., and ...
Within the trimeric S protein, only one of the three RBD heads is present in the accessible conformation to bind the human ... protein, nucleocapsid (N) protein, membrane (M) protein and the envelope (E) protein, each of which is essential to compose the ... Exposure of the RBD in the S1 protein subunit creates an unstable subunit conformation. Consequently, during binding, S1 ... Proteins and Peptides. Proteomics tools. Agonists, activators, antagonists and inhibitors. Cell lines and Lysates. Multiplex ...
... normally folded protein to adopt this disease-associated conformation when introduced into an organism. [9] Spontaneous ... Second, the transmitting agent is a misfolded protein called the prion protein, capable of causing native, ... Lewy bodies comprise a number of different aggregated proteins, the most diagnostically useful of which is alpha-synuclein. [20 ... Amyloid angiopathy can be identified using stains for amyloidal protein (Congo red, thioflavin-S), or immunohistochemical ...
The conformation of Escherichia coli ribosomal protein L7/Ll2 in solution: hydrodynamic, spectro¬scopic, and conformation ... Altered erythrocyte membrane proteins in sickle cell patients associated with the severity of the disease. Biochem. Med. 19:95 ... Isolation and characterization of fatty acid binding protein in the liver of the nurse shark, Ginglymostoma cirratum. Comp. ... The conformational stability of ribosomal protein L7/Ll2: The effects of pH, temperature and guani¬dinium chloride. ...
... normally folded protein to adopt this disease-associated conformation when introduced into an organism. [9] Spontaneous ... Second, the transmitting agent is a misfolded protein called the prion protein, capable of causing native, ... Lewy bodies comprise a number of different aggregated proteins, the most diagnostically useful of which is alpha-synuclein. [20 ... Amyloid angiopathy can be identified using stains for amyloidal protein (Congo red, thioflavin-S), or immunohistochemical ...
Moreover, cryo-electron microscopy showed that the mAb could bind to RBD in the spike proteins up and down conformations. ... P2G3 showed the highest binding affinity for the spike protein from ancestral SARS-CoV-2 and a panel of Alpha, Beta, Gamma, and ... The latest VOC, Omicron, carries 37 mutations in its spike protein, most of which lie within the receptor-binding domain (RBD ... In contrast, when Omicron spike protein was used, P2G3 was three-fold more potent than P5C3. ...
Alushin studies how the wiggly protein strands known as actin filaments bend and flex, crisscross each other, and have tugs of ... Alushin studies how the wiggly protein strands known as actin filaments bend and flex, crisscross each other, and have tugs of ... But trying to capture the conformations of proteins using X-ray crystallography, which was the standard methodology back then, ... The first step in studying a proteins shape was to coax it into forming a crystal-and so many proteins refused to crystallize ...
... puts these ssDNA sequences into optimal conformations for interacting with DNA polymerases and other replication proteins. By ... T4 Gene 32 Protein. T4 Gene 32 Protein. For increasing PCR amplification and DNA sequencing efficiency. ... The native Gene 32 Protein from bacteriophage T4 (T4gp32) is a single-stranded DNA binding protein that is required for T4 DNA ... The T4 Gene 32 Protein is a single-stranded nucleic acid binding protein that has the function of stabilizing single-stranded ...
Efficient Construction of Disordered Protein Ensembles in a Bayesian Framework with Optimal Selection of Conformations. Pacific ... Using Intramolecular Disulfide Bonds in Tau Protein to Deduce Structural Features of Aggregation-resistant Conformations. ... Predicting Protein Structure with Probabilistic Models. In: Protein Structural Biology in Bio-Medical Research , Vol. 22B of ... Protein Science. 2006; 15: 2166-2177.. Stultz CM. Cosmology and proteins: landscape of possibilities. Nature Physics. 2006; 2(6 ...
Photoactivated chromophore conformation in Photoactive Yellow Protein (E46Q mutant) from 10 microseconds to 3 milliseconds. ... Photoactivated chromophore conformation in Photoactive Yellow Protein (E46Q mutant) from 10 to 500 nanoseconds. ... Click on the protein counts, or double click on taxonomic names to display all proteins containing PAS domain in the selected ... WILD TYPE PHOTOACTIVE YELLOW PROTEIN, P63 AT 295K. 1otd. STRONG HYDROGEN BONDS IN PHOTOACTIVE YELLOW PROTEIN AND THEIR ROLE IN ...
All the latest science news about protein-protein interactions from Phys.org ... and hinges can generate distinctive conformations that are important for protein function. Most proteins perform their ... To fulfill their diverse functions, they have to interact with other proteins. Such protein-protein interactions are mediated ... Deep learning for new protein design. The key to understanding proteins-such as those that govern cancer, COVID-19, and other ...
... the outcome of regulatory proteins that leads to changes in the life span of an mRNA ... folding that leads to proteins with alternative conformations d. ... folding that leads to proteins with alternative conformations d ... the outcome of regulatory proteins that leads to changes in the life span of an mRNA. ...
I have taken few conformations of a ligand(same ligand)from Protein Data Bank. I want to calculate RMSD of these conformations ...
Broadly used in modern drug design, molecular docking methods explore the ligand conformations adopted within the binding sites ... The most likely binding conformation and the corresponding intermolecular interactions are identified. The protein backbone is ... Protein Sci. 2015. Epub ahead of print. [Google Scholar] [CrossRef] [PubMed]. *Lin, J.H. Accommodating protein flexibility for ... Moreira, I.S.; Fernandes, P.A.; Ramos, M.J. Protein-protein docking dealing with the unknown. J. Comput. Chem. 2010, 31, 317- ...
... and the proteins native conformation/charge was altered, based on electrophoretic mobility. Three types of modification were ... a major carrier protein for MDI in vivo. LC-MS/MS analysis of GSH-MDI reaction products identified products possessing the ... protein antigens, which may participate in pathogenic inflammatory responses. To test this hypothesis, an occupationally ...
... either by affecting the conformation of specific proteins or by exacerbating local oxidative stress. The apparently critical ... The iron cannot be removed from the blood before transfusion, as it is a critical component of hemoglobin, a protein in red ... notably decreased the levels of protein-HNE adducts.. The authors stated that these findings have important implications ... The Cochrane systematic evidence review found 1 RCT (n = 36) of metal protein attenuating compounds in AD. That trial, of ...
... identifying novel anthropomorphic molecules targeting multiple receptor conformations; and identifying EF hand protein S100 as ... The team hopes to develop an app to solve protein-protein interaction puzzles. ... The primary focus of Rajnarayanans research team is to design and develop molecules that target functionally relevant protein ... Rajnarayanans team has developed human computer interface (HCI) devices using 3-D printed protein models to generate ...
  • Furin cleavage at the S1/S2 site may lead to conformational changes in the viral S protein that exposes the RBD and/or the S2 domain. (abcam.com)
  • Consequently, during binding, S1 undergoes conformational rearrangement between two states, known as the up and down conformations. (abcam.com)
  • We, therefore, need continuous descriptions of protein conformational space in the form of energy landscapes in order to properly understand their mechanisms of action. (europa.eu)
  • 1980. The conformational stability of ribosomal protein L7/Ll2: The effects of pH, temperature and guani¬dinium chloride. (mote.org)
  • Burger V., Arenas D., Stultz CM. A Structure-free Method for Quantifying Conformational Flexibility in proteins. (mit.edu)
  • The high-affinity interaction of LF with pore-forming outer-membrane proteins (OMPs) of Gram-negative enterics, including Escherichia coli , is critical for the antimicrobial outcome of LF (Gado et al. (ift.org)
  • 1979. The conformation of Escherichia coli ribosomal protein L7/Ll2 in solution: hydrodynamic, spectro¬scopic, and conformation prediction studies. (mote.org)
  • These thermosensors are part of a regulatory network, such as the production of heat shock proteins mediated by sigma factor 32 (RpoH) in Escherichia coli or the transcriptional repressor of heat-shock genes HrcA in Bacillus subtilis (Hecker et al. (springer.com)
  • Actin filaments power cellular movement, bind with hundreds of different cellular components, and serve as tracks for molecular motor proteins. (rockefeller.edu)
  • The T4 Gene 32 Protein is intended for molecular biology applications. (qiagen.com)
  • A screening technique commonly used in drug discovery can yield important details about the actions of molecular 'glues' in protein interactions. (phys.org)
  • Proteins are the key players for virtually all molecular processes within the cell. (phys.org)
  • Due to the inherent diversity in the underlying mechanisms, protein-based thermosensors affect different cellular processes such as transcription, translation, protein stability, signal transduction as well as proteolytic processes. (springer.com)
  • The alpha/beta fold, which differs from the original chain tracing, shows striking similarity to distinct parts of the signal transduction proteins profilin and the SH2 domain. (embl.de)
  • Overall, the high-resolution structure of photoactive yellow protein supports a mechanism whereby electrostatic interactions create an active site poised for photon-induced rearrangements and efficient protein-mediated signal transduction. (embl.de)
  • AD is characterized diagnostically by two histologic findings: (1) extracellular amorphus eosinophilic deposits of amyloid consisting of Aβ peptides (a cleavage product of amyloid precursor protein [APP]), which are referred to as amyloid plaques, and (2) intraneuronal aggregates of abnormally modified microtubule-associated protein tau (neurofibrillary tangles) (see the image below). (medscape.com)
  • The peptide unit is modeled by trans-N -methylacetamide (NMA) which is allowed to interact with various hydrogen bonding species that are similar to those typically found in the environment of a peptide within a protein molecule. (usu.edu)
  • Protein separation conditions always pose the risk of denaturation or structural alteration of the LF molecule. (ift.org)
  • 1994). The highly cationic N-terminus region of LF could facilitate charge-induced protein aggregation and inactivate the molecule. (ift.org)
  • Inheritance of some variant alleles causes a change in conformation of the alpha-1 antitrypsin molecule, leading to polymerization and retention within hepatocytes. (msdmanuals.com)
  • PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). (bvsalud.org)
  • The third class of thermosensing is based on the temperature-dependent conformation of specific RNA sequences, which are termed RNA-thermometer (RNAT). (springer.com)
  • This binding puts these ssDNA sequences into optimal conformations for interacting with DNA polymerases and other replication proteins. (qiagen.com)
  • Fisher C., Ullman O., Stultz CM., Comparative Studies of Disordered Proteins with Similar Sequences: Application to AB40 and AB42. (mit.edu)
  • Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. (cdc.gov)
  • The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. (bvsalud.org)
  • Temperature has a direct effect on fundamental biological systems, including enzyme activity and correct folding of proteins. (springer.com)
  • Changes in temperature are typically sensed as a result of conformation changes of protein structure as well as misfolded proteins. (springer.com)
  • 6, 7, 8] Alteration in protein conformation with temperature changes also leads to decreased solubility and subsequent vasculitic damage. (medscape.com)
  • He shifted his focus from microtubules to actin filaments, another key part of the cytoskeleton made up of long polymers of proteins linked end-to-end. (rockefeller.edu)
  • Activated lactoferrin (ALF) is a new form of a naturally occurring protein from milk that acts as a powerful deterrent to pathogenic bacteria that may be present on a meat surface. (ift.org)
  • The interaction of LF with microbial surfaces-OMPs of Gram-negative bacteria in particular-has led to other antimicrobial mechanisms, such as the inhibition of microbial attachment to sub-epithelial matrix proteins and detachment of bacteria from mucosal surfaces. (ift.org)
  • Many different principles of thermoregulation have been identified in bacteria, which can be assigned to the class of protein-, DNA- or RNA-thermosensors. (springer.com)
  • SARS-CoV-2 S protein binds to the ACE2 receptor at the surface of host cells, initially through the S1 RBD. (abcam.com)
  • In addition to binding ACE2, increasing evidence suggests that SARS-CoV-2 can also bind other surface proteins to gain cell entry. (abcam.com)
  • In a subsequent angiotensin-converting enzyme 2 (ACE2)-spike surrogate neutralization assay, P5C3, and P2G3 exhibited broad and highly potent inhibition of binding (of VOC spike proteins) to ACE2. (news-medical.net)
  • Many possess genes that encode proteins to neutralize the affects of antibiotics and prevent attacks on their cell machinery. (icr.org)
  • They also intrigued him because they seemed to merge a classical way to think about biology-as a system of genes and proteins-with the lesser understood concept of mechanobiology, "occupying an existential gray area between the microscopic chemical and the macroscopic physical worlds," Alushin says. (rockefeller.edu)
  • The shape of things to come: structural insights into how prion proteins encipher heritable information. (cdc.gov)
  • The SARS-CoV-2 genome encodes four major structural proteins: the spike (S) protein, nucleocapsid (N) protein, membrane (M) protein and the envelope (E) protein, each of which is essential to compose the viral particle 3 . (abcam.com)
  • Proteins are dynamic entities that undergo many structural transitions and fluctuations, which are essential to their biological functions. (europa.eu)
  • Hybrid methods that combine computational biophysics with experimental structural biology have proved successful in describing protein conformation, namely their 3D shape. (europa.eu)
  • Walker S., Ullman O., Stultz CM. Using Intramolecular Disulfide Bonds in Tau Protein to Deduce Structural Features of Aggregation-resistant Conformations. (mit.edu)
  • There are 613402 PAS domains in 396128 proteins in SMART's nrdb database. (embl.de)
  • Early in the pandemic, variants of SARS-CoV-2 containing the D614G mutation in the spike (S) protein that increases receptor binding avidity rapidly became dominant in many geographic regions ( 5 , 6 ). (cdc.gov)
  • A protein called p63, which is closely related to another protein that suppresses the formation of tumors, plays an essential role in detecting and responding to DNA damage. (elifesciences.org)
  • The down state transiently hides the RBD, while the up state exposes the RBD, but temporarily destabilizes the protein subunit 7 , 8 , 9 . (abcam.com)
  • Riek R , Hornemann S , Wider G , Billeter M , Glockshuber R , Wüthrich K . NMR structure of the mouse prion protein domain PrP(121-231). (cdc.gov)
  • 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. (embl.de)
  • The 1.4 A crystallographic structure of photoactive yellow protein, determined by multiple isomorphous replacement methods, provides the first view at atomic resolution of a protein with a photocycle. (embl.de)
  • In the dark state structure of photoactive yellow protein, the novel 4-hydroxycinnamyl chromophore, covalently attached to Cys69, is buried within the major hydrophobic core of the protein and is tethered at both ends by hydrogen bonds. (embl.de)
  • The T4 Gene 32 Protein has exhibited an ability to enhance the performance of several DNA synthesis-related activities in secondary-structure rich regions, including PCR amplification and DNA sequencing. (qiagen.com)
  • Burger V., Nolasco D., Stultz CM., Expanding the Range of Protein Function at the Far end of the Order-Structure Continuum. (mit.edu)
  • Linder D., Gurry T., Stultz CM. Towards a Consensus in Protein Structure Nomenclature. (mit.edu)
  • Stultz CM. Protein Structure along the order-disorder continuum. (mit.edu)
  • The key to understanding proteins-such as those that govern cancer, COVID-19, and other diseases-is quite simple: Identify their chemical structure and find which other proteins can bind to them. (phys.org)
  • To test this hypothesis, an occupationally relevant dose of MDI (0.1%w/v) was reacted with varying concentrations of GSH (10µM-10mM), and the reaction products were characterized with regard to mass/structure, and ability to carbamoylate human albumin, a major carrier protein for MDI in vivo. (cdc.gov)
  • The TRIP13 gene provides instructions for making a protein that has several roles in cell division. (medlineplus.gov)
  • TRIP13 gene mutations involved in MVA syndrome lead to production of an abnormally short protein that is quickly broken down. (medlineplus.gov)
  • The native Gene 32 Protein from bacteriophage T4 (T4gp32) is a single-stranded DNA binding protein that is required for T4 DNA replication, recombination and repair. (qiagen.com)
  • The T4 Gene 32 Protein also stimulates the rate of synthesis of T4 DNA Polymerase on primed-single-stranded substrates showing a 5-10-fold increase in synthesis rate. (qiagen.com)
  • The T4 Gene 32 Protein is a single-stranded nucleic acid binding protein that has the function of stabilizing single-stranded regions of DNA. (qiagen.com)
  • The ability of T4 Gene 32 Protein to enhance the performance of several DNA synthesis-related activities is based on its essential function in the replication of bacteriophage T4. (qiagen.com)
  • Instructions for using T4 Gene 32 Protein are provided in the corresponding kit protocol in the resources below. (qiagen.com)
  • DNA binding of single stranded DNA by T4 Gene 32 Protein was measured using a gel shift assay with a single-stranded, fluorescently labeled oligonucleotide. (qiagen.com)
  • Protein concentration (OD 280 ) of T4 Gene 32 Protein was determined by OD 280 absorbance. (qiagen.com)
  • Ribosomes, the structures where protein synthesis is catalyzed, are the targets of many other Streptomyces antibiotics such as spectinomycin, tetracycline, and streptomycin. (icr.org)
  • Back then, electron microscopy methods to study structures were in their infancy, so one of the things we had to do was to take pictures of proteins using photographic film," he says. (rockefeller.edu)
  • He spent many nights alone in a pitch-black lab, utterly silent, utterly still, as he attempted to record protein structures on film, not daring to breathe lest the vibrating air make the image blurry. (rockefeller.edu)
  • Dear amber users, I have taken few conformations of a ligand(same ligand)from Protein Data Bank. (vanderbilt.edu)
  • These variants carry a constellation of genetic mutations, including in the S protein receptor-binding domain, which is essential for binding to the host cell angiotensin-converting enzyme-2 (ACE-2) receptor to facilitate virus entry. (cdc.gov)
  • This protein contains two subunits: the S1 subunit that contains the receptor-binding domain (RBD) and N-terminal domain (NTD), and a second S2 subunit that mediates the fusion of the viral and host cell membranes 4 . (abcam.com)
  • The latest VOC, Omicron, carries 37 mutations in its spike protein, most of which lie within the receptor-binding domain (RBD), the target for neutralizing antibodies (nAbs). (news-medical.net)
  • While high temperatures account for denatured and misfolded proteins, low temperatures may cause damage to membranes. (springer.com)
  • 1991. Isolation and characterization of fatty acid binding protein in the liver of the nurse shark, Ginglymostoma cirratum. (mote.org)
  • P2G3 showed the highest binding affinity for the spike protein from ancestral SARS-CoV-2 and a panel of Alpha, Beta, Gamma, and Delta spike proteins . (news-medical.net)
  • Improved yields and quality of templates may be achieved with the use of DNA-binding proteins in amplification and sequencing reactions. (qiagen.com)
  • The antimicrobial functionality of LF is dependent on its protein conformation and milieu conditions (Naidu and Arnold, 1997). (ift.org)
  • A shortage of this protein impairs the spindle assembly checkpoint, and cell division proceeds, even if not all the chromatids are attached to spindle microtubules. (medlineplus.gov)
  • Spectinomycin and tetracycline prevent proteins from being assembled by the cell and streptomycin induces the assembly of the wrong amino acids into the translated protein. (icr.org)
  • 5,6] Without proteins, which are necessary for normal cell function, the cell dies. (icr.org)
  • TMPRSS2 cleavage of the SARS-CoV-2 S protein is believed to enable the fusion of the viral capsid with the host cell to permit viral entry 5 , 6 . (abcam.com)
  • Within the trimeric S protein, only one of the three RBD heads is present in the accessible conformation to bind the human Angiotensin 2 (hACE2) host cell receptor 10 . (abcam.com)
  • Both Neuropilin-1 and Neuropilin-2 have been shown to bind the cleaved form of the SARS-CoV-2 S protein to mediate host cell entry 13, 14 . (abcam.com)
  • 1978. Altered erythrocyte membrane proteins in sickle cell patients associated with the severity of the disease. (mote.org)
  • Alushin studies how these little-understood physical dynamics act on the cell's cytoskeleton, an internal network of protein filaments that constantly reconfigures itself to help the cell move, change shape, or ferry molecules from one cell compartment to another. (rockefeller.edu)
  • The protein then switches to an active form when DNA damage is detected to trigger the process of cell self-destruction. (elifesciences.org)
  • In contrast, when Omicron spike protein was used, P2G3 was three-fold more potent than P5C3. (news-medical.net)
  • The spike protein of SARS-CoV--a target for vaccine and therapeutic development. (who.int)
  • This process is dependent upon activation of the S protein, by cleavage at two sites (S1/S2 and S2') via the proteases Furin and TMPRSS2. (abcam.com)
  • Funded by the Marie Skłodowska-Curie Actions programme, the EnLaCES project will present a new hybrid methodology that leverages recent innovations in cryogenic electron microscopy to examine the continuous dynamics and energy landscapes of large, multi-domain proteins. (europa.eu)
  • In this proposal, we present a new hybrid methodology that leverages recent innovations in cryo-electron microscopy image analysis to examine continuous dynamics and free energy landscapes of large, multi-domain proteins, which are not achievable with existing methods. (europa.eu)
  • Protein dynamics through motions of loops, linkers, and hinges can generate distinctive conformations that are important for protein function. (phys.org)
  • Exposure of the RBD in the S1 protein subunit creates an unstable subunit conformation. (abcam.com)
  • Cellular stress, or oxidative stress, occurs when there is a buildup of reactive oxygen species (ROS), which interferes with cellular mechanisms and can even cause damage to proteins, lipids, and DNA. (phys.org)
  • All species are found to have a restricting influence on the conformation of a peptide bond. (usu.edu)
  • The TRIP13 protein appears to regulate this checkpoint, although the exact mechanism is unclear. (medlineplus.gov)
  • the remaining patients are probably able to degrade the abnormal protein, although the exact protective mechanism is unclear. (msdmanuals.com)
  • Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. (embl.de)
  • Taxonomic distribution of proteins containing PAS domain. (embl.de)
  • The complete taxonomic breakdown of all proteins with PAS domain is also avaliable . (embl.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing PAS domain in the selected taxonomic class. (embl.de)
  • One conserved NAC domain was analyzed in all the NAC proteins. (bvsalud.org)
  • also found that the oocytes of mice already contain all the proteins necessary to activate p63. (elifesciences.org)
  • Incomplete glycosylation during prion infection unmasks a prion protein epitope that facilitates prion detection and strain discrimination. (cdc.gov)
  • Imperiali B. Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation. (mit.edu)
  • 4] Failure of DNA to properly separate during these processes results in a bacterium not being able to divide normally or produce functional proteins. (icr.org)
  • Upon co-incubation of GSH-MDI reaction products with human albumin, MDI was rapidly transferred to specific lysines of albumin, and the protein's native conformation/charge was altered, based on electrophoretic mobility. (cdc.gov)
  • Streptomyces-produced quinolone and coumarin antibiotics, such as novobiocin, interfere with a protein called gyrase that assists in the normal separation of double-stranded DNA during replication of DNA or transcription of messenger RNA. (icr.org)
  • Theoretical Studies of Environmental Effects on Protein Conformation. (usu.edu)
  • Theoretical Studies of Environmental Effects on Protein Conformation: Flexibility of the Peptide Bond S. Scheiner and C. W. Kern J. Am. Chem. (usu.edu)
  • Arg52, located in a concavity of the protein surface adjacent to the dominant patch of negative electrostatic potential, shields the chromophore from solvent and is positioned to form a gateway for the phototactic signal. (embl.de)
  • The first step in studying a protein's shape was to coax it into forming a crystal-and so many proteins refused to crystallize, making success "a bit too random for my taste," he says. (rockefeller.edu)
  • As a result, cells lack TRIP13 protein. (medlineplus.gov)
  • Most proteins perform their functions in cells. (phys.org)
  • In a study of patients with type II cryoglobulinemia, peripheral blood mononuclear cells from 18 patients were separated into CD3+ (T cells), CD19+ (B cells), and CD14+ (monocytes) and analyzed for the presence of negative-strand HCV RNA and for HCV nonstructural protein 3 (NS3). (medscape.com)
  • NS3 protein was also detected in 6 patients: 5 were positive in T cells, 3 in B cells, and 3 in monocytes. (medscape.com)
  • Shortly after SARS-CoV emerged at the turn of the 21st century, the spike (S) protein (particularly in its native conformation) was identified as the immunodominant antigen of the virus3. (who.int)
  • This means that once the switch to the active form is triggered there is no delay waiting for other proteins to be made, which makes oocytes extremely sensitive to DNA damage. (elifesciences.org)
  • Purity was assessed by comparing the aggregate mass of contaminant bands in the concentrated sample to the mass of the protein of interest band in the diluted sample. (qiagen.com)