Amino Acid Sequence: 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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Molecular Sequence Data: 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.Cloning, Molecular: 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.Amino Acids: 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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Sequence Homology, Nucleic Acid: The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.Sequence Alignment: 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.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Escherichia coli: 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.Cyanogen Bromide: Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.Amino Acid Substitution: 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.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Molecular Weight: The sum of the weight of all the atoms in a molecule.Genes, Bacterial: The functional hereditary units of BACTERIA.DNA: 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).Recombinant Proteins: Proteins prepared by recombinant DNA technology.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.Protein Conformation: 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).Trypsin: 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 Proteins: Proteins found in any species of bacterium.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Species Specificity: The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Genes: A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Sequence Analysis: A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Mutation: 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.Peptides: 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.Kinetics: The rate dynamics in chemical or physical systems.Open Reading Frames: A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Amino Acid Motifs: 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.Amino Acids, Essential: Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Chymotrypsin: 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.Amino Acid Transport Systems: Cellular proteins and protein complexes that transport amino acids across biological membranes.Gene Library: A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Cattle: 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.Conserved Sequence: 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.Structure-Activity Relationship: 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.Blotting, Northern: Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.DNA, Bacterial: Deoxyribonucleic acid that makes up the genetic material of bacteria.Protein Structure, Tertiary: 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.Codon: A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).DNA Primers: 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.Polymerase Chain Reaction: 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.Proteins: 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.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Protein Binding: 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.Recombinant Fusion Proteins: 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.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Blotting, Southern: A method (first developed by E.M. Southern) for detection of DNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.Protein Structure, Secondary: 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.Macromolecular Substances: 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.Chromatography, Ion Exchange: Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Sequence Analysis, Protein: 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.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Multigene Family: A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)Rabbits: 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.Chickens: 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.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Saccharomyces cerevisiae: 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.Thermolysin: A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) Mapping: Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.DNA Restriction Enzymes: Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of DNAs, and have made it possible to splice and recombine genes from one organism into the genome of another. EC 3.21.1.Amino Acids, Branched-Chain: Amino acids which have a branched carbon chain.Sequence Homology: The degree of similarity between sequences. Studies of AMINO ACID SEQUENCE HOMOLOGY and NUCLEIC ACID SEQUENCE HOMOLOGY provide useful information about the genetic relatedness of genes, gene products, and species.Nucleic Acid Hybridization: Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503)Membrane Proteins: 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.Viral Proteins: Proteins found in any species of virus.Amino Acids, Aromatic: Amino acids containing an aromatic side chain.Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Oligonucleotide Probes: Synthetic or natural oligonucleotides used in hybridization studies in order to identify and study specific nucleic acid fragments, e.g., DNA segments near or within a specific gene locus or gene. The probe hybridizes with a specific mRNA, if present. Conventional techniques used for testing for the hybridization product include dot blot assays, Southern blot assays, and DNA:RNA hybrid-specific antibody tests. Conventional labels for the probe include the radioisotope labels 32P and 125I and the chemical label biotin.Epitopes: Sites on an antigen that interact with specific antibodies.Genetic Complementation Test: A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.Amino Acids, SulfurProtein PrecursorsProtein Sorting Signals: Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.Evolution, Molecular: The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.Chromosome Mapping: Any method used for determining the location of and relative distances between genes on a chromosome.Swine: Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).Genes, Fungal: The functional hereditary units of FUNGI.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Biological Evolution: The process of cumulative change over successive generations through which organisms acquire their distinguishing morphological and physiological characteristics.Enzyme Stability: 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.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Genes, Viral: The functional hereditary units of VIRUSES.Carboxypeptidases: Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.Chromatography, Affinity: A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Hydrogen-Ion Concentration: 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)Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.Lysine: An essential amino acid. It is often added to animal feed.Alanine: 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.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Sequence Deletion: Deletion of sequences of nucleic acids from the genetic material of an individual.Fungal Proteins: Proteins found in any species of fungus.Mutagenesis: Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.Protein Processing, Post-Translational: 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.Consensus Sequence: A theoretical representative nucleotide or amino acid sequence in which each nucleotide or amino acid is the one which occurs most frequently at that site in the different sequences which occur in nature. The phrase also refers to an actual sequence which approximates the theoretical consensus. A known CONSERVED SEQUENCE set is represented by a consensus sequence. Commonly observed supersecondary protein structures (AMINO ACID MOTIFS) are often formed by conserved sequences.Tissue Distribution: Accumulation of a drug or chemical substance in various organs (including those not relevant to its pharmacologic or therapeutic action). This distribution depends on the blood flow or perfusion rate of the organ, the ability of the drug to penetrate organ membranes, tissue specificity, protein binding. The distribution is usually expressed as tissue to plasma ratios.Genomic Library: A form of GENE LIBRARY containing the complete DNA sequences present in the genome of a given organism. It contrasts with a cDNA library which contains only sequences utilized in protein coding (lacking introns).Oligodeoxyribonucleotides: 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.Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Isoelectric Point: The pH in solutions of proteins and related compounds at which the dipolar ions are at a maximum.Temperature: 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.RNA: 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)DNA-Binding Proteins: Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Genetic Variation: Genotypic differences observed among individuals in a population.Glycine: A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.Isoleucine: An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.Glycosylation: 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.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Proline: 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.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Oligopeptides: Peptides composed of between two and twelve amino acids.Bacillus: A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.Pepsin A: Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Arginine: An essential amino acid that is physiologically active in the L-form.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Organ Specificity: Characteristic restricted to a particular organ of the body, such as a cell type, metabolic response or expression of a particular protein or antigen.Point Mutation: 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.Blotting, Western: 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.Chromatography: Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.COS Cells: CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)Exons: The parts of a transcript of a split GENE remaining after the INTRONS are removed. They are spliced together to become a MESSENGER RNA or other functional RNA.Trypsin Inhibitors: Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.Electrophoresis, Paper: Electrophoresis in which paper is used as the diffusion medium. This technique is confined almost entirely to separations of small molecules such as amino acids, peptides, and nucleotides, and relatively high voltages are nearly always used.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Solubility: 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)Carbohydrates: The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.Oxidoreductases: The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Operon: In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.Glutamine: A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.Circular Dichroism: 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)Aspartic Acid: 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.Amino Acid Transport Systems, Basic: Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).DNA, Fungal: Deoxyribonucleic acid that makes up the genetic material of fungi.DNA, Recombinant: Biologically active DNA which has been formed by the in vitro joining of segments of DNA from different sources. It includes the recombination joint or edge of a heteroduplex region where two recombining DNA molecules are connected.Genetic Code: The meaning ascribed to the BASE SEQUENCE with respect to how it is translated into AMINO ACID SEQUENCE. The start, stop, and order of amino acids of a protein is specified by consecutive triplets of nucleotides called codons (CODON).Glycoside HydrolasesImmunoblotting: Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.Cross Reactions: Serological reactions in which an antiserum against one antigen reacts with a non-identical but closely related antigen.Amino Acids, Basic: Amino acids with side chains that are positively charged at physiological pH.Capsid: The outer protein protective shell of a virus, which protects the viral nucleic acid.Ferredoxins: Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.Tryptophan: 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.Valine: A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.Plants, Medicinal: Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals.Repetitive Sequences, Nucleic Acid: Sequences of DNA or RNA that occur in multiple copies. There are several types: INTERSPERSED REPETITIVE SEQUENCES are copies of transposable elements (DNA TRANSPOSABLE ELEMENTS or RETROELEMENTS) dispersed throughout the genome. TERMINAL REPEAT SEQUENCES flank both ends of another sequence, for example, the long terminal repeats (LTRs) on RETROVIRUSES. Variations may be direct repeats, those occurring in the same direction, or inverted repeats, those opposite to each other in direction. TANDEM REPEAT SEQUENCES are copies which lie adjacent to each other, direct or inverted (INVERTED REPEAT SEQUENCES).Amino Acids, DiaminoPseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Mutagenesis, Insertional: Mutagenesis where the mutation is caused by the introduction of foreign DNA sequences into a gene or extragenic sequence. This may occur spontaneously in vivo or be experimentally induced in vivo or in vitro. Proviral DNA insertions into or adjacent to a cellular proto-oncogene can interrupt GENETIC TRANSLATION of the coding sequences or interfere with recognition of regulatory elements and cause unregulated expression of the proto-oncogene resulting in tumor formation.Fabaceae: The large family of plants characterized by pods. Some are edible and some cause LATHYRISM or FAVISM and other forms of poisoning. Other species yield useful materials like gums from ACACIA and various LECTINS like PHYTOHEMAGGLUTININS from PHASEOLUS. Many of them harbor NITROGEN FIXATION bacteria on their roots. Many but not all species of "beans" belong to this family.Streptomyces: A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value.Bacterial Outer Membrane Proteins: Proteins isolated from the outer membrane of Gram-negative bacteria.Serine: A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Geobacillus stearothermophilus: A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.Threonine: An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.Bacillus subtilis: A species of gram-positive bacteria that is a common soil and water saprophyte.Genome, Viral: The complete genetic complement contained in a DNA or RNA molecule in a virus.ChitinaseDNA Mutational Analysis: Biochemical identification of mutational changes in a nucleotide sequence.Capsid Proteins: Proteins that form the CAPSID of VIRUSES.DNA, Viral: Deoxyribonucleic acid that makes up the genetic material of viruses.Introns: Sequences of DNA in the genes that are located between the EXONS. They are transcribed along with the exons but are removed from the primary gene transcript by RNA SPLICING to leave mature RNA. Some introns code for separate genes.Gene Expression Regulation: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.Muscles: Contractile tissue that produces movement in animals.Lectins: Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.Isoelectric Focusing: Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.Viral Structural Proteins: Viral proteins that are components of the mature assembled VIRUS PARTICLES. They may include nucleocapsid core proteins (gag proteins), enzymes packaged within the virus particle (pol proteins), and membrane components (env proteins). These do not include the proteins encoded in the VIRAL GENOME that are produced in infected cells but which are not packaged in the mature virus particle,i.e. the so called non-structural proteins (VIRAL NONSTRUCTURAL PROTEINS).Nitrogen: An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.Repetitive Sequences, Amino Acid: A sequential pattern of amino acids occurring more than once in the same protein sequence.Promoter Regions, Genetic: DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.Binding, Competitive: 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.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.

*  Which of the following terms refers to a sequence of amino acids coiling into a...
Which of the following terms refers to a sequence of amino acids coiling into a helix or folding into pleats as a result of ... Mutations that change the amino acid sequence of a polypeptide often result in the production of a defective protein. Defective ... The sequence of the amino acids in a protein is referred to as ... When amino acids are joined together to form a polypeptide ... If there were a mutation in a ribosome that prevented tRNA molecules from moving into the E site, how many amino ...
*  5HT1A Receptor peptide (228-240) (ab45743) | Abcam
SequenceC-KTVKKVEKTGADT. *Amino acids228 to 240. Specifications. Our Abpromise guarantee covers the use of ab45743 in the ... Sequence similaritiesBelongs to the G-protein coupled receptor 1 family. 5-hydroxytryptamine receptor subfamily. HTR1A sub- ...
*  Recombinant human Hsp60 protein (ab78430) | Abcam
Amino Acid Sequence *SpeciesHuman. Associated products. *Related Products. *Anti-Hsp60 antibody [Mab11-13] (ab13532) ...
*  Human PPP2R5A peptide (ab22797) | Abcam
Amino Acid Sequence *SpeciesHuman. *SequenceC-AYNMHSILSNTSAE. *Amino acids473 to 486 ... Sequence similaritiesBelongs to the phosphatase 2A regulatory subunit B56 family.. *Post-translational. modifications ...
*  Recombinant Human Phospholamban protein (ab114227)
Amino Acid Sequence *AccessionP26678. *SpeciesHuman. *SequenceMEKVQYLTRSAIRRASTIEMPQQARQKLQN. *Molecular weight29 kDa including ... Sequence similaritiesBelongs to the phospholamban family.. *Post-translational. modificationsPhosphorylation by PKA abolishes ...
*  Recombinant Human Otx1 protein (ab114691) | Abcam
Amino Acid Sequence *AccessionP32242. *SpeciesHuman. *SequenceYGMNGLGLAGPAMDLLHPSVGYPATPRKQRRERTTFTRSQLDVLEALFAK ... Sequence similaritiesBelongs to the paired homeobox family. Bicoid subfamily.. Contains 1 homeobox DNA-binding domain. ...
*  Pesticide Factory: Bt-toxins Produced in GM Corn
In 1998, an FDA researcher discovered that Cry1Ab shared a sequence of 9-12 amino acids with vitellogenin, an egg yolk allergen ...
*  TEAS 5 test scores 10 points lower than older version??? | allnurses
Also, sequencing of dna amino acids.. like a with t and stuff like that. Oh yea and there are some weird direction and order ... things too... like this sequence: WKYTES then a series of 10 steps like take out every third letter, replace each vowel with an ...
*  Genbank HBVrt References
Download amino acid sequences: aligned. Download nucleic acid sequences: aligned or unaligned. ...
*  Marine Drugs | Free Full-Text | First Report of a Peroxiredoxin Homologue in...
The full-length cDNA sequence of CcPrx4 consisted of 884 nucleotides with an open reading frame encoding a mature protein of ... 247 amino acids. It showed a significant homology to peroxiredoxin 4 (Prx4) with the highly conserved F-motif (93FTFVCPTEI101 ... Multiple sequence alignment of the CcPrx4 amino acid sequence with other known Prx4 amino acid sequences from the GenBank ... Multiple sequence alignment of the CcPrx4 amino acid sequence with other known Prx4 amino acid sequences from the GenBank
*  Patent US5008240 - Method of treating inflammation - Google Patents
2 The method of claim 1 wherein the cartilage inducing factor or functional equivalent is a homodimer whose chains do not have a the following partial N-terminal amino acid sequence: Ala-Leu-Asp-Thr-Asn-Tyr-Cys-Phe-Ser-Ser-Thr-Glu-Lys-Asn-Cys-Cys-Val-Arg-Gln-Leu-Tyr-Ile-Asp-Phe-Arg-Lys-Asp-Leu-Gly-Trp, or b The following partial N-terminal amino acid sequence: Ala-Leu-Asp-Ala-Ala-Tyr-Cys-Phe-Arg-Asn-Val-Gln-Asp-Asn-Cys-Cys-Leu-Arg-Pro-Leu-Tyr-Ile-Asp-Phe-Lys-Arg-Asp-Leu-Gly-Trp-. The method of claim 15 wherein the cartilage inducing factor or functional equivalent is a homodimer whose chains each have a the following partial N-terminal amino acid sequence: Ala-Leu-Asp-Thr-Asn-Tyr-Cys-Phe-Ser-Ser-Thr-Glu-Lys-Asn-Cys-Cys-Val-Arg-Gln-Leu-Tyr-Ile-Asp-Phe-Arg-Lys-Asp-Leu-Gly-Trp-, or b the following partial N-terminal amino acid sequence: ...
*  Interleukin-10 Antibodies
OF THE INVENTION Provided herein is a humanized recombinant antibody molecule that binds IL-10, or binding fragment thereof, comprising: at least one antibody light chain variable region, or binding fragment thereof, comprising a polypeptide having at least one amino acid sequence selected from the group consisting of SEQ ID NO:1 at CDR1, SEQ ID NO:2 at CDR2, and SEQ ID NO:3 at CDR3; and a framework region, wherein the amino acid sequence of framework region is all or substantially all of a human immunoglobin amino acid sequence; and at least one antibody heavy chain variable region, or binding fragment thereof, comprising a polypeptide having at least one amino acid sequence selected from the group of SEQ ID NO:6 at CDR1, SEQ ID NO:7 at CDR2, and SEQ ID NO:8 at CDR3; and a framework region, wherein the amino acid sequence of framework region is all or substantially all of a human immunoglobin ...
*  National Biomedical week in Dialysis Technology Forum
... Yuku free message boards Username or E-mail: Password:. Forgot Password. Sign Up Grab the Yuku app. Search:. Dialysis Technologists Dialysis Technology National Biomedical week. 0 Points. Search this Topic:. Remove this ad. Add Reply. New Topic. New Poll. Forum Jump Dialysis Technology. Video Uploads. Career Opportunities. Core Competencies and Standards Review. Archived Dialysis Technology. Relevant Dialysis Articles. . Previous Topic. Next Topic. . National Biomedical week. Author Comment. Marc Heroux National Biomedical week. Lead. Posts : 644 May 20 12 4:38 PM. Reply. Quote. More. My Recent Posts. Tags : None National Biomedical/Clinical Engineering Appreciation Week This year Biomed/CE National Appreciation Week takes place May 20 - 26, 2012. We encourage all organization departments to celebrate. This can be done in the following ways:. • set up a booth and/or display with photos and information; • hold an open house; • contact your local TV affiliate; • deliver a presentation; • celebrate at a ...
*  Patente US5814441 - HTLV-I and HTLV-II peptide antigens and methods - Google Patentes
Matsushita, S., et al., Proc Natl Acad Sci USA, 83:2672 1986. J., et al., Proc Natl Acad Sci USA, 77:7415 1980. P., et al., Science, 226:1094 1984. T et al., Science, 249:386 1990. Seiki, M., et al., Proc Natl Acad Sci USA, 80:3618 1983. The region is contained in a 41 amino acid sequence overlap of three gp46 peptide antigens, designated MTA-1, MTA-4, and MTA-5. 6 shows the HTLV-II coding sequence, and corresponding amino acid sequence in the region of the gp46 envelope protein from which HTLV-II peptides of the invention are derived; and FIG. A HTLV-I Derived Peptides In one embodiment, the peptides contain the immunogenic region from the 41-amino acid overlap region from above-described MTA-1, MTA-4, and MTA-5 HTLV-I peptides. Secondly, a comparison of the amino acid sequence of MTA-1 peptide with the corresponding region in the HTLV-II gp46 protein FIG. The peptides are derived from the HTLV-II gp46 envelope protein ...
*  Patent US7575738 - Heat shock protein as a targeting agent for endothelium-specific in vivo ... - Go
The Heat Shock Protein may be labeled with imaging agents that are capable of binding lectin-like oxidized low-density lipoprotein LOX-1 or may be attached to a therapeutic agent. The Heat Shock Protein may be labeled with imaging agents that are capable of binding lectin-like oxidized low-density lipoprotein LOX-1 or may be attached to a therapeutic agent. Thus, the moiety that binds to LOX-1 can be synthesized using known techniques, given the known amino acid sequence of the LOX-1 polypeptide. The term peptides is usually used to refer to those containing less than 100 amino acids with a molecular weight of about 10,000 Da. Definitions As used herein, Heat Shock Protein of the embodiments of the invention may be referred to throughout the application as the ligand, the peptide sequence, HSP, the LOX-1 binding peptide, or the binding peptide. A composition as used herein, refers broadly to any composition containing a described molecule, peptide, or amino ...
*  Protein sequencing
... The two major direct methods of protein sequencing are mass spectrometry and the Edman degradation reaction. Protein sequencer Determining amino acid composition Hydrolysis. 'N'-terminal amino acid analysis C-terminal amino acid analysis Edman degradation Digestion into peptide fragments. Mass spectrometry Predicting protein sequence from DNA/RNA sequences Bioinformatics tools for sequencing See also References Further reading. 'N'-terminal amino acid analysis. File:Sanger peptide end-group analysis.svg|thumb|360px|Sanger's method of peptide end-group analysis: 'A' derivatization of 'N'-terminal end with Sanger's reagent DNFB, 'B' total acid hydrolysis of the dinitrophenyl peptide Determining which amino acid forms the 'N'-terminus of a peptide chain is useful for two reasons: to aid the ordering of individual peptide fragments' sequences into a whole chain, and because the first round of Edman ...
*  Plant peptide hormone
It was found to be an 18-amino acid peptide processed from the C-terminus of a 200-amino acid precursor, which is called prosystemin. 1 CLV3 /ESR-related 'CLE' peptide family — 'CLV3' encodes a small secreted peptide that functions as a short range ligand to the membrane-bound CLV1 receptor like kinase that together with CLV2 a receptor-like protein function to maintain stem cell homeostasis in 'Arabidopsis' shoot apical meristems. 2 and CLV3 are very different, they are both members of the CLE peptide family given that they share a short conserved 14-amino acid sequence at the carboxy terminal region. 3 To date, more than 150 CLE signaling peptides are identified. 6 ENOD40 — is an early nodulin gene, hence ENOD, that putatively encodes two small peptides, one of 12 and the other of 18 amino acid residues. The bioactive five amino acid peptide PSK is proteolytically processed from an ~80 amino acid precursor secreted ...
*  Structural motif
... Motifs do not allow us to predict the biological functions: they are found in proteins and enzymes with dissimilar functions. Because the relationship between primary structure and tertiary structure is not straightforward, two biopolymers may share the same motif yet lack appreciable primary structure similarity. In most DNA motifs, for example, it is assumed that the DNA of that sequence does not deviate from the normal " double helical " structure. Structural motifs in proteins See also References Further reading. Structural motifs in proteins. In proteins, a structural motif describes the connectivity between secondary structural elements. An individual motif usually consists of only a few elements, e.g., the 'helix-turn-helix' motif which has just three. Note that, while the 'spatial sequence' of elements may be identical in all instances of a motif, they may be encoded in any order within the underlying gene. In addition to secondary structural elements, protein structural motifs ...
*  SMART: Secondary literature for DPBB 1 domain
Each subunit contains nine beta-strands and three alpha-helices;it is folded into the double-psi beta-barrel structure. Further,detailed sequence comparison, aided by examination of the crystalstructure of the DNA-dependent RNA polymerase DDRP, showed that the RDRPand the beta' subunit of DDRP and its orthologs in archaea andeukaryotes contain a conserved double-psi beta-barrel DPBB domain. The deduced amino acid sequence of LipL41 would encode a355-amino-acid polypeptide with a 19-amino-acid signal peptide, followedby an L-X-Y-C lipoprotein signal peptidase cleavage site. 1996; 178 : 1146-53 Display abstract The degQ and degS genes of Escherichia coli encode proteins of 455 and 355residues, respectively, which are homologs of the DegP protease. The gene product contains anamino-terminal signal sequence to direct the protein for secretion and aconsensus lipoprotein modification sequence. Ichikawa JK, Li C, Fu J, Clarke S A gene at ...
*  Protein Processing I
... : Targeting to the Endomembrane System. Newly synthesized proteins enter the endomembrane system through the endoplasmic reticulum. A targeting sequence of hydrophobic amino acids near the N- terminal end of the growing polypeptide results in the binding of the ribosome to ER membrane and in insertion of the polypeptide into the endoplasmic reticulum. Let's deal first with the case of proteins that will be inserted into the ER lumen : The signal sequence is a long sequence of about 20 hydrophobic amino acid residues that contains a hydrophobic membrane crossing domain at the N terminal end. The ribosome becomes attached to a ribosome receptor that also functions as the translocation channel for the newly synthesized polypeptide. Proteins inserted into membranes : Two categories of hydrophobic signals used in insertion of membrane proteins. Start transfer sequences. Unlike the N-terminal signal sequence, it is not cleaved after transfer of the ...
*  Patent US7960508 - Peptide having cytotoxicity inhibitory activity and method of screening ... - Goo
More preferably, the peptide fragment or a series of the peptide fragments according to the present invention has the amino acid sequence of the formula: Arg Ser Xaa Cys Cys His Cys Arg His Leu Ile Phe Glu Lys SEQ ID NO: 1 wherein Xaa represents selenocysteine, or said amino acid sequence with one or several amino acid residues therein being deleted, substituted or added, or a partial sequence of either of the above amino acid sequences, or an amino acid sequence comprising as a part any of the above amino acid sequences. The present inventors confirmed that a peptide fragment having the amino acid sequence: Lys Arg Cys Ile Asn Gln Leu Leu Cys Lys Leu Pro Thr Asp Ser Glu Leu Ala Pro Arg Ser Xaa Cys Cys His Cys Arg His Leu Ile Phe Glu Lys SEQ ID NO: 3 wherein Xaa represents selenocysteine had the cytotoxicity-inhibitory activity, which peptide fragment was purified ...
*  Protein Structural Levels Tutorial
The shape of a protein is typically described using four levels of structural complexity: the primary, secondary, tertiary, and quaternary structural levels. Protein Primary Structure The primary structure of a protein is its amino acid sequence. Each protein has a unique amino acid sequence, and the unique order in which the amino acids are linked together determined the higher levels of structural organization. The primary structure of the -subunit of human hemoglobin is shown below. What are the first 10 amino acids in this polypeptide chain. Some segments do not have similar and angles for all amino acids in the segment. Rotate the molecule around and observe the distribution of secondary structures in the -subunit of human hemoglobin. Similarly each of the other secondary structure elements present in the protein is composed of residues that are adjacent to each other in sequence. The -subunit of human hemoglobin ...
*  KDEL (amino acid sequence)
kdel amino acid sequence kdel amino acid sequence kdel is a target peptide sequence in the amino acid structure of a protein which prevents the protein from being secreted from the endoplasmic reticulum er a protein with a functional kdel motif will be retrieved from the golgi apparatus by retrograde transport to the er lumen it also targets proteins from other locations such as the cytoplasm to the er proteins can only leave the er after this sequence has been cleaved off the abbreviation kdel is formed by the corresponding letters to each amino acid this letter system was defined by the iupac and iubmb in and is as follows k lysine d aspartic acid e glutamic acid l leucine therefore the sequence in three letter code is lys asp glu leu see also er retention kkxx amino acid sequence endoplasmic reticulum protein retention receptors kdelr kdelr kdelr references category amino ...
*  Fun People Archive - 20 Jan - A Scientific Sighting
... Fun People Archive 20 Jan A Scientific Sighting. Date: Fri, 20 Jan 95 14:14:39 PST From: Peter Langston psl> To: Fun People Subject: A Scientific Sighting Forwarded-by: lanih@irony.Berkeley.EDU Lani Herrmann Forwarded-by: Alix Herrmann Scheurer> further forwards eaten, originator lost BMW. Examination of nucleic acid and protein sequences compiled in computer databases has lead to many significant findings of homology between sequences and shared sequence motifs among divergent organisms. We wish to report the discovery of a sequence motif of potentially great importance which is shared by proteins from a number of organisms. The motif consists of the amino acid sequence Glu-Lys-Val-Ile-Ser; or, in the one letter amino acid code, "ELVIS." We examined the Protein Identification Resource, National Biomedical Research Foundation NBRF protein database release no. Of 25814 sequences contained in this release, ...
*  C6orf58
Genomic DNA Length base pairs Exon s Mature mRNA Length base pairs Splice variants Signal peptide Coding region CDS base pair. Species Common Name Accession Number Sequence Length base pairs Sequence Identity. Amino acid length amino acids signal peptide Signal Peptide Length amino acids. Molecular Weight of Precursor Protein Molecular Weight of Signal Peptide Predicted Molecular Weight of Mature Peptide predicted Molecular Weight observed Isoelectric Point Predicted N-linked glycosylation Site. Mass spectrometry has shown that the observed molecular weight of UPF0762 is 32kDa. 7 It remains unclear why the observed molecular weight is less than predicted, even after accounting for cleavage of the signal peptide. Species Common Name Accession Number Sequence Length amino acids Sequence Identity % Sequence Similarity %. Observed post-translational modifications include N-linked glycosylation at amino acid ...
*  Protein structure
Domains, motifs, and folds in protein structure Structural domain. Structural and sequence motif. Protein folding Protein structure determination Structure classification Computational prediction of protein structure See also References Further reading. thumb|right|250px|'Protein structure', from primary to quaternary structure. Amino acid residues. Amino acid. The primary structure of a protein refers to the linear sequence of amino acids in the polypeptide chain. The two ends of the polypeptide chain are referred to as the carboxyl terminus C-terminus and the amino terminus N-terminus based on the nature of the free group on each extremity. One chain has 31 amino acids, and the other has 20 amino acids. thumb|right|100px|An alpha-helix with hydrogen bonds yellow dots. The folding is driven by the 'non-specific' hydrophobic interactions, the burial of hydrophobic residues from water, but the structure is stable only ...
*  KIAA0922
'Transmembrane protein 131-like' TMEM131L protein, alternatively named 'uncharacterized protein KIAA0922' KIAA0922 protein, is an integral transmembrane protein encoded by the human gene 'KIAA0922' that is significantly conserved in eukaryotes, at least through protists. Furthermore, its paralog, prolyl endopeptidase PREP whose function is known, provides clues as to the function of TMEM131L. Gene mRNA Protein Expression. There is only one confirmed transmembrane domain region in protein TMEM131L. This domain exists near the center of the protein, at 871-891 amino acid of the 1610 amino acid long protein sequence for isoform I. There is also a switch to a higher density of predicted N-linked glycosylation sites across this confirmed transmembrane region 0.0136 to 0.0069 predicted N-glycosylation sites/amino acid at this region. Furthermore, the only confirmed phosphorylation site is on the latter half of the protein 1,123 aa in isoform I and predicted ...
*  Nonpolar-amino-acid-transporting ATPase
nonpolar amino acid transporting atpase nonpolar amino acid transporting atpase in enzymology a nonpolar amino acid transporting atpase is an enzyme that catalyzes the chemical reaction atp h o nonpolar amino acidout rightleftharpoons adp phosphate nonpolar amino acidin the substrates of this enzyme are atp h o and nonpolar amino acid whereas its products are adp phosphate and nonpolar amino acid this enzyme belongs to the family of hydrolase s specifically those acting on acid anhydrides to catalyse transmembrane movement of substances the systematic name of this enzyme class is atp phosphohydrolase nonpolar amino acid transporting references category ec category enzymes of unknown structure
*  Baldwin Estate Mortise Locksets
toll free 866.366.4066 atlanta 770.623.1530 Phone sales until 8:00pm M-TH, 5:30pm F. door hardware. cabinet hardware. FILTER RESULTS 003 Lifetime Polished Brass 031 Non Lacquered Brass 050 Satin Brass & Black 055 Lifetime Polished Nickel 056 Lifetime Satin Nickel 102 Oil Rubbed Bronze charcoal Black 112 Venetian Bronze 260 Polished Chrome 402 Distressed Oil Rubbed Bronze Baldwin Solid Brass - Select the Finish. home > all categories > Door Hardware > BALDWIN > Baldwin ESTATE LOCKSETS > BALDWIN ESTATE MORTISE LOCK THUMBLATCH ENTRY SETS. Baldwin KENSINGTON 3/4 ESCUTCHEON MORTISE ENTRY - 2 1/2" WIDTH. Baldwin 6401.402 5.5 Center to Center Bore - Tubular - DEVONSHIRE ENTRANCE SET - DISTRESSED OIL RUBBED BRONZE 6401 $507.50. Baldwin 6401.003 5.5 Center to Center Bore Tubular - DEVONSHIRE ENTRANCE SET - LIFETIME POLISHED BRASS $507.50. Baldwin 6401.055 5.5 Center to Center Bore Tubular - DEVONSHIRE ENTRANCE SET - LIFETIME POLISHED NICKEL $507.50. Baldwin 6401.031 5.5 Center to Center Bore, Tubular - DEVONSHIRE ... BALDWIN ESTATE MORTISE LOCK THUMBLATCH ENTRY SETS
*  Advances in Protein Chemistry and Structural Biology | 978-0-12-386483-3 | Elsevier
Advances in Protein Chemistry and Structural Biology. Elsevier. Skip to content Feedback Menu. Products - Book. Info/Buy View on ScienceDirect. Advances in Protein Chemistry and Structural Biology Edited by Rossen Donev, Swansea University, Swansea, Wales, UK Published continuously since 1944, the Advances in Protein Chemistry and Structural Biology serial has been a continuous, essential resource for protein chemists. Covering reviews of methodology and research in all aspects of protein chemistry, including purification/expression, proteomics, modeling and structural determination and design, each volume brings forth new information about protocols and analysis of proteins while presenting the most recent findings from leading experts in a broad range of protein-related topics. This volume features articles on Protein Aggregation. View full description. Audience Biochemists, biophysicists, cell biologists, protein chemists, structural geneticists, and structural biologists. Book information Published: ...
*  Protein, Proteins
Proteins are made of amino acids linked into linear chains, called polypeptide chains. Amino acids links between each other by peptide bonds - this peptide bond is formed between the carboxyl and amino groups of neighbouring amino acids. Proteins are formed by one or several polypeptide chains. There are only 20 standard amino acids are exists in living organism. Sometimes these amino acids are chemically modified in the protein after protein synthesis. For example for 10 amino acid sequence it is possible to have 20 10 different sequences, which is approximately equal to 10 13 or 10 trillions of different structures. The structures build from 2 to 100 amino acids with molecular weight up to 10 kDa are usually called peptides. Protein in living organisms Generally speaking, proteins do everything in the living cells. All functions of the living organisms are related with proteins. ...
*  New Page 1
The molecular evolutionary clock hypothesis may be defined as the thesis that changes in amino acid sequence of a specific protein proceed at a constant rate in regard to time. T he molecular evolutionary clock hypothesis may be defined most simply as the hypothesis that changes in amino acid sequence in a specific functional protein proceed at a constant rate in regard to time. In the definition of the molecular evolutionary clock hypothesis, it is important to note the words specific and functional since the apparent rate of change is different for different proteins, and the function of the protein has been considered to be the primary constraint on the rate of change. Although initially the molecular clock concept was based on sequences in functional proteins, and in genes for those proteins, more recently it has been extended to include segments of DNA e.g., PSEUDOGENES, INTRONS, etc. Historically, the concept of a constant change of rate with time was ...
*  OmpT
'OmpT' is an aspartyl protease found on the outer membrane of ' Escherichia coli '. 1 Structure Mechanism Biological function and disease relevance Urinary tract infections. Evolved suicidal action of OmpT. coli'. 3 Genetic differences between OmpT and other members of the omptin family are found in the extracellular loops, and therefore, this area is thought to be associated with substrate specificity. thumb|left|Schematic representing the residues on OmpT that mediate the nucleophilic attack of water during peptide cleavage. The substrate of OmpT binds to negatively charged aspartate and glutamate residues, so the active site of the protease is anionic. This causes OmpT to selectively cleave peptides between two basic positively charged residues. 5 The most common bond cleavage by OmpT is between two arginine residues because their positive charge can favorably interact with the negatively charged species at the active site during substrate binding. 6 Because of the specificity of the active site, OmpT ...
*  Patent US5877151 - Method for inhibiting production of tumor necrosis factor - Google Patents
10 is a graph comparing the effects of endotoxin and CAP37 peptide 20-44 on cardiac index in the hyperdynamic model of septic shock. 15 is a graph comparing the effects of endotoxin and CAP37 peptide 20-44 on cardiac index in the hypodynamic model of septic shock. In another version of the invention, the composition may comprise a peptide comprising a subunit of the amino acid sequence defined in the Sequence Listing of SEQ ID NO:1, for example, having the amino acid sequence as defined in the Sequence Listing of SEQ ID NO:2. In another version of the invention, the composition may comprise a peptide having the amino acid sequence as defined in the Sequence Listing of SEQ ID NO:3, or an effective subunit thereof. The invention further contemplates a peptide capable of binding to bacterial lipopolysaccharide, comprising the amino acid sequence as defined in the Sequence Listing of SEQ ID NO:1 or SEQ ...
*  Syndecan
The ectodomains show the least amount of amino acid sequence conservation, not more than 10–20%; in contrast, the transmembrane and cytoplasmic domains share approximately 60–70% amino acid sequence identity. 4 The transmembrane domains contain an unusual alanine/glycine sequence motif, while the cytoplasmic domain is essentially composed of two regions of conserved amino acid sequence C1 and C2, separated by a central variable sequence of amino acids that is distinct for each family member V. For example, in mouse cells and tissues, syndecan 1 is highly expressed in fibroblastic and epithelial cells. Syndecan 2 is highly expressed in endothelial, neural, and fibroblastic cells, whereas it has low expression levels in epithelial cells. Syndecan 3 is highly expressed in neural cells, but has low or undetectable amount in epithelial cells. Syndecan 4 is highly expressed by epithelial and fibroblastic cells, but has low ...
*  What is the known number of amino acids that form proteins ? - Homework Help -
What is the known number of amino acids that form proteins. - Homework Help - Homework Help. Essay Lab. Study Tools ▻. Literature Guides. Quizzes. eTexts. Teachers ▻. For Teachers. Literature Lesson Plans. Literature Quizzes. Sign In. Join. Sign In. Join. What is the known number of amino acids that form proteins. Asked on June 17, 2013 at 4:43 PM. dislike 0. Level 3 Educator Emeritus. Posted on June 17, 2013 at 5:06 PM Answer #1. There exists 20 required amino acids and they are known such that: essential, nonessential and conditional. There exists 8 essential aminoacids that need to be obtained from the food. They are called "essential" because of the fact that the body cannot produce them and they need to be aquired from the daily diet. The nonessential aminoacids are produced by the body and not from daily diet. There exists 4 nonessential aminoacids such that: glutamic acid, aspartic ...
*  The Internal Sequence of the Peptide-Substrate Determines Its N-Terminus Trimming by ERAP1
... Evnouchidou, Irini ; Momburg, Frank ; Papakyriakou, Athanasios ; Chroni, Angeliki ; Leondiadis, Leondios ; Chang, Shih-Chung ; Stratikos, Efstratios ; Goldberg, Alfred L. Note: Order does not necessarily reflect citation order of authors. Evnouchidou, Irini, Frank Momburg, Athanasios Papakyriakou, Angeliki Chroni, Leondios Leondiadis, Shih-Chung Chang, Alfred L. Goldberg, and Efstratios Stratikos. The internal sequence of the peptide-substrate determines Its N-terminus trimming by ERAP1. ERAP1 has unique properties for an aminopeptidase being able to trim peptides in vitro based on their length and the nature of their C-termini. We discovered strong internal sequence preferences of peptide N-terminus trimming by ERAP1. Preferences were only found for positively charged or hydrophobic residues resulting to trimming rate changes by up to 100 fold for single residue substitutions and more than 40,000 fold for multiple residue substitutions for peptides with identical N-termini. ...
*  Coronin
7 The WD-repeat is a structural motif comprising approximately 40 amino acids usually ending with the amino acid sequence tryptophan W – aspartic acid D and hence the name WD. These domains were discovered in 1986 and are characterized by a partial conserved domain of 40-60 amino acids, starting with GH dipeptide 11-24 residue away from the N-terminus and ending with a tryptophane-aspartic acid WD dipeptide at the C-terminus. WD repeat proteins have diverse cellular functions. Apart from the core domain, almost all coronins have a short conserved N-terminal motif and coiled coil motif of 50 amino acids at the C-terminus. The N-terminal region contains 12 basic amino acids which can be taken as signature as it is present in only coronin proteins. Furthermore, each coronin contains a unique divergent region between the WD domain and C-terminal coiled coil region. The unique region of 'Dictyostelium' has 22 amino ...
The method of claim 10, wherein the composition further comprises any one or both of: a a substantially purified polypeptide comprising an amino acid sequence having at least 80% sequence identity to any one of SEQ ID NOs:10-12, or to an antigenic fragment thereof and b a substantially purified polypeptide comprising an amino acid sequence having at least 80% sequence identity to any one of SEQ ID NOs:13-15, or to any one of SEQ ID NOs: 16-18, or to an antigenic fragment thereof. The method of claim 18, wherein the composition further comprises any one or both of: a a substantially purified polypeptide comprising an amino acid sequence having at least 80% sequence identity to any one of SEQ ID NOs:10-12, or to an antigenic fragment thereof; and b a substantially purified polypeptide comprising an amino acid sequence having at least 80% sequence identity to any one of SEQ ID NOs:13-15, or to any one ...
*  EPO - T 0128/92 () of 30.11.1994
Moreover, the Appellant had not made credible that the combination of any of documents 23 and 19 with one of documents 27, 28 or 29 would allow a full length cDNA coding for IL-2 to be picked up: another team see documents 39 and 43 used a different route to that of the patent and did not obtain a full length cDNA coding for IL-2. None of the prepublished documents cited by the Appellant disclosed any IL-2 amino acid sequence nor demonstrated that this had been made available to the public before the priority date of the patent. The Board thus accepts neither the IL-2 nor the monoclonal antibody as something that can be treated as made available to the public within the meaning of Article 54 2 EPC. In order to do this, the full length cDNA coding for IL-2 had to be picked up from a cDNA library with a method that did not involve oligonucleotide probes, as no IL-2 amino acid sequence information was available. The skilled person could have started from the enriched ...
*  MIPS database availability
... POSTMAST at GUNBRF.BITNET POSTMAST at GUNBRF.BITNET. Tue Jun 2 15:01:00 EST 1992. Previous message: linetest only Next message: Unique Numerical Protein Representation Messages sorted by:. A list of the PIR entries for the known and hypothetical protein sequences located on yeast chromosome III is available by sending the command SEND YEASTC3.LIS in the body of a mail message to FILESERV at GUNBRF on BITNET. All the entries listed in the returned file are currently available in PIR2 and can be retrieved by sending a command like GET PIR2:S19337 to the same address. There are 182 entries in the list with codes from S19337 through S19518. Because of file size limitations imposed by the BITNET network, all of those entries cannot be retrieved in one request. Requests of about 20 entries at most should be retrieved with each request. ------------------------------------------------------------------------ Dr. John S. Garavelli Database Coordinator Protein Identification Resource National Biomedical ...
*  Transmembrane protein 53
... 'Transmembrane protein 53', or 'TMEM53', is a protein that is encoded on chromosome 1 in humans. 1 It has no paralogs but is predicted to have many orthologs across eukaryotes. DUF829 makes up 87% of TMEM53's length Contains a transmembrane domain but lacks a signal peptide Molecular weight 31.6 kilodaltons Isoelectric point 8.56 Leucine-rich 14.4% of amino acids are leucines Predicted to be localized to the nucleus. AceView Splice Form Amino Acids % ID with RefSeq of Clones Found DUF829 CK2 sites PKC sites Tyr sites Pumilio site N-Myristoylation sites Extras not comparable to RefSeq. It contains a domain of unknown function, 'DUF829', which is approximately 240 amino acids long. This domain has not been found in proteins other than TMEM53 and its orthologs. Expressed at lower levels in brain tissue with Huntington's disease than in normal brain tissue. Transmembrane protein 53 has no paralogs. 277 aa. 204 aa. 278 aa. 276 aa. 405 aa. 276 aa. 285 aa. Based on ...
*  Protein microsequencing
... dmeier at mis mcw edu dmeier at mis mcw edu tue aug est previous message polyclar at next message yep primers urgent messages sorted by hello all to sequence the amino terminal end of a peptide a facility in wisconsin requires pmol of protein if the protein is approx daltons then sequencing requires micrograms of pure protein is that typical for protein sequencing facilities i d appreciate your replies dan meier previous message polyclar at next message yep primers urgent messages sorted by more information about the methods mailing list
*  Siah interacting protein N-terminal domain
siah interacting protein n terminal domain siah interacting protein n terminal domain in molecular biology the protein domain siah interacting protein n terminal domain is found at the n terminal of the protein siah interacting protein sip it has a helical hairpin structure with a hydrophobic core which is further stabilised by an arrangement of side chain s contributed by the two amphipathic helices the function of this domain remains to be fully elucidated but it is known to be vital for interactions with siah it has also been hypothesised that sip can dimerise through this n terminal domain function sip protein the sip protein has a role as an adaptor protein it links the e ubiquitin ligase activity of siah with skp and ebi f box protein in the degradation of beta catenin a transcriptional activator of tcf lef genes this is important for signalling that the protein needs to undergo proteolysis at the s proteosome n terminal domain of sip protein more specifically the n terminal domain of the sip protein ...
*  Baldwin 6931 Baldwin Baldwin DALLAS MORTISE ENTRY SET - 1 5/8" X 14" EXTERIOR 6931 at Door Hardware
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*  Baldwin 6931 Baldwin Baldwin DALLAS MORTISE ENTRY SET - 1 5/8" X 14" EXTERIOR 6931 at Door Hardware
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*  Terminal amine isotopic labeling of substrates
... 'Terminal amine isotopic labeling of substrates' 'TAILS' is a method in quantitative proteomics that identifies the protein content of samples based on N-terminal fragments of each protein N-terminal peptide s and detects differences in protein abundance among samples. Like other methods based on N-terminal peptides, this assay uses trypsin to break proteins into fragments and separates the N-terminal peptides the fragments containing the N-termini of the original proteins from the other fragments internal tryptic peptides. Alternative methods that rely on the free amino group of the N-terminus to identify the N-terminal peptides cannot detect some N-termini because they are "naturally blocked" i.e. This assay isolates the N-terminal peptides by removing the internal tryptic peptides via ultrafiltration leaving the labeled mature N-terminal and neo-N-Terminal peptides to be analyzed by tandem mass spectrometry MS/MS. Alternative methods that rely on the free amino group of the N-terminus ...
*  Discovery of Functional Components of Proteins from Amino-Acid Sequences based on Rough Sets and Hie
discovery of functional components of proteins from amino acid sequences based on rough sets and hierarchical reasoning discovery of functional components of proteins from amino acid sequences based on rough sets and hierarchical reasoning shusaku tsumoto and hiroshi tanaka protein structure analysis from dna sequences is an important and fast growing area in both computer science and biochemistry although interesting approaches have been studied it is very difficult to capture the characteristics of protein since even a simple protein are made of more than amino acids which makes biochemical experiments very difficult to detect functional components for this reason almost all the problems in this field are left unsolved and it is very important to develop a system which assists researchers on molecular biology to remove the difficulties caused by combinatorial ezplasions in this paper we report a system called mola ...
*  TIM Barrel Analysis
The eight-stranded a / b barrel TIM barrel is by far the most common tertiary fold observed in high resolution protein crystal structures. In this study, an analysis has been attempted on proteins which were found to have the a/b structural motif to study their structural features like conformational preferences, functional significance, topological features such as solvent accessibility, residue preference, salt bridges, sequence similarity etc. The lack of substantial sequence homology between members of this family makes it a challenging target for evolutionary analysis and to trace the ancestry of each member of this class. The barrel region was then analysed for features like solvent accessibility, salt bridges, geometric features like length of major and minor axis etc using programs developed inhouse coded in Fortran 77 by Prof. Dataset for study:. One of the most intriguing features among members of this class of proteins is although they all exhibit the same tertiary fold there is very ...
*  Nancy Scarola | Baldwin, NY Real Estate Agent | Realtor Profile & Listings
Nancy Scarola. Baldwin, NY Real Estate Agent. 3 br 4 br +. Advanced Min Baths 1 Baths 2 Baths 3 Baths 4 Baths 5 Baths 6 Baths. License No: 10311200650 Service areas: Baldwin, North Baldwin, Freeport, Baldwin Harbor. About Nancy Scarola Nancy Scarola is an elite New York real estate agent, ranked in the upper 9% of her peers at the 91st percentile. Nancy's brokerage of record is Nancy Scarola Real Estate Inc where she primarily serves sellers with Single Family properties in Baldwin, North Baldwin and Freeport. Nancy stands out because of her depth of experience as a listing agent and her ability to negotiate a lower price per square foot for her buyers relative to the buyers of comparable properties. Experienced Nancy has significantly more experience than other real estate agents in the Baldwin area who list and sell similar homes. Speedy Closer Nancy is quicker than his peers at getting his listings sold for his clients. 260 Meister Blvd Freeport, NY 11520 Single Family 2538 SQ FT, $183/SQ FT. 2805 Laurel ...
*  Baldwin 6942 Baldwin BISMARK MORTISE ENTRY SET - 1 7/8" X 8 3/8" at Door Hardware
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... 'Mitochondrial-processing peptidase subunit beta' is an enzyme that in humans is encoded by the 'PMPCB' gene. This protein is located in the mitochondrial matrix and catalyzes the cleavage of the leader peptides of precursor proteins newly imported into the mitochondria, though it only functions as part of a heterodimeric complex. Structure Function Interactions Clinical significance References Further reading. The Mitochondrial-processing peptidase subunit beta precursor protein is 54.4 KDa in size and composed of 489 amino acids. The precursor protein contains a 45 amino acid N-terminal fragment as mitochondrion targeting sequence. After cleavage, the matured PMPCB protein is 49.5 KDa in size and has a theoretical pI of 5.76. Mitochondrial-processing peptidase MPP is a metalloendopeptidase, containing two structurally related subunits, mitochondrial-processing peptidase subunit alpha and subunit beta, working in conjunction for its catalytic function. 3 Containing ...
'Mitochondrial-processing peptidase subunit alpha' is an enzyme that in humans is encoded by the 'PMPCA' gene. This gene 'PMPCA' encoded a protein that is a member of the peptidase M16 family. This protein is located in the mitochondrial matrix and catalyzes the cleavage of the leader peptides of precursor proteins newly imported into the mitochondria, though it only functions as part of a heterodimeric complex. Structure Function Interactions Clinical significance References Further reading. The Mitochondrial-processing peptidase subunit alpha precursor protein is 58.2 KDa in size and composed of 525 amino acids. The precursor protein contains a 33 amino acid N-terminal fragment as mitochondrion targeting sequence. After cleavage, the matured PMPCA protein is 54.6 KDa in size and has a theoretical pI of 5.88. Mitochondrial-processing peptidase MPP is a metalloendopeptidase, containing two structurally related subunits, Subunit alpha and mitochondrial-processing peptidase ...
A lipopeptide consisting of the following amino acid sequence: L-Glu-X-D-Leu-L-Val-L-Asp-D-Leu-L-Leu SEQ ID NO: , wherein X is any amino acid, and wherein the lipopeptide comprises a fatty acid moiety on the L-Glu residue. In some embodiments, the lipopeptide has the following amino acid sequence: L-Glu-X-D-Leu-L-Val-L-Asp-D-Leu-L-Leu SEQ ID NO: , wherein X is any amino acid, and wherein the lipopeptide comprises a fatty acid moiety on the L-Glu residue. In certain embodiments, the lipopeptide has the following amino acid sequence: L-Leu-D-Leu-L-Val-L-Asp-D-Leu-L-Leu SEQ ID NO: , wherein the lipopeptide comprises a fatty acid moiety on the L-Leu residue. The downstream sequence was obtained from pUC19-1CD-48DR-1HG, pUC19-1CD-78DR-1HG, pUC19-1CD-102DR-1HG using primers 1HG-and-2HG-BglI-FW: 5′-ATTACTACGCCTCTCTGGCACACAACATACGAGCCGGAAGCATAAAGTG-3′ SEQ ID NO: , and ...
*  Baldwin Hardware 4764.151.CD Baldwin Switch Plate - iQHardware
... Toll Free: 1-888-988-9220 M-F 8am-5pm EST. FREE Standard Shipping on Orders $100 or More. Search Products. Home. Shipping Returns. Track My Order. My Account. About Us. Search. Checkout. . Baldwin Switch Plate. Back to product. Home. Baldwin Hardware. General Hardware Baldwin Hardware. Switch Plates Baldwin Hardware. SKU: 4764.151.CD Manufacturer:. Baldwin Hardware Baldwin Switch Plate. Availability: In Stock Price: $6.30. Quantity:. Previous. Next. Questions about the Baldwin Hardware 4764.151.CD. Send us an email for more information. Description Finishes Reviews. Baldwin Switch Plate Classic Cable Cover - Prod Code: .CD = Item blister packed on a card - Finish 151 Antique Nickel. View Content No Reviews For This Product. OUR VENDORS. 0 Item s in cart. Total $0.00. Checkout. PRODUCT LOCATORS Baldwin HW Locator. Emtek / Epitome HW Locator. Von Morris HW Locator. Yale HW Locator. NAVIGATION Entrysets. Mortise Entrance Handlesets. Brass Mortise Entrance Handlesets. Wrought Steel Mortise Entrance ...
*  Baldwin Hardware 4750.150.CD Baldwin Switch Plate - iQHardware
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*  Role of Unc51.1 and its binding partners in CNS axon outgrowth. Genes Dev
The first, SynGAP, a negative regulator of Ras, is expressed within axons and growth cones of developing granule cells. The first, SynGAP, a negative regulator of Ras, is expressed within axons and growth cones of developing granule cells. Although the C?-terminal 399 amino acids of Unc51.1 amino acids 653–1051, as well as the shorter C?-terminal domain of Unc51.1 amino acids 829–1051, strongly bound SynGAP, the spacer region amino acids 653–828 and subregions of the C?-terminal domain amino acids 829–1001 and amino acids 913–1051 did not bind SynGAP. The bait regions of Unc51.1 amino acids 653–1051 and Unc51.2 amino acids 531–1037 were fused in-frame with a GST tag and tested for binding to theC?-terminal region of 829–1328 and its deletion mutants, D1 and D2 amino acids 829–1053 and amino acids 1054–1328, respec- tively. In these assays, GST–Unc51.1 and GST–Unc51.2 ...
*  Complete Protein? Complete Nonsense. ~ Angela Raines | elephant journal
Complete Protein. Complete Protein. 4 Complete protein is a myth. While all animal foods contain all of those 8 amino acids, not all plant foods do or, rather, some plant foods contain one in only trace amounts. 88143 50 Responses Complete+Protein%3F+Complete+Nonsense. 2010-10-07+15%3A49%3A29 Angela+Raines to Complete Protein. You can not gain unhealthy weight eating vegetables- only refined carbs, unhealthy fats, and animal products. AngelaRaines says: October 7, 2010 at 23:27 Carrie, were you vegetarian during your pregnancy. elephantjournal says: April 25, 2011 at 13:49 via elephantjournal says: April 29, 2011 at 10:13 # Steven B: Good article. Perhaps it is a myth that complete proteins are a necessary component of diet, but it is an equally persistent and discredited myth in some circles that ...
*  NIF | Searching in Literature
NIF. SciCrunch relies heavily on JavaScript. Many functions on the site will not work if you continue with JavaScript disabled. NIF LinkOut Portal. Add a Resource. Literature. X Forgot Password. If you have forgotten your password you can enter your email here and get a temporary password sent to your email. Leaving Community. Leaving the community will revoke any permissions you have been granted in this community. Literature. Home Literature. The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1. Here we report the 2.2 A crystal structure of RhoA bound to an effector domain of protein kinase PKN/PRK1. The structure reveals the antiparallel coiled-coil finger ACC finger fold of the effector domain that binds to the Rho specificity-determining regions containing switch I, beta strands B2 and B3, and the C-terminal alpha helix A5, predominantly by specific hydrogen bonds. The ACC finger fold is distinct from those for ...
*  Baldwin 6520 Baldwin Baldwin BRISTOL SECTIONAL MORTISE SET - 2 1/2" WIDTH 6520 at Door Hardware USA.
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*  Post-translational modification - Psychology Wiki
Wikia. Skip to Content Skip to Wiki Navigation Skip to Site Navigation. Search this wikia Search all of Wikia. Psychology Wiki Navigation On the Wiki. Edit this Page. Edit. Posttranslational modification is the chemical modification of a protein after its translation. During protein synthesis, 20 different amino acids can be incorporated in proteins. After translation, the posttranslational modification PTM of amino acids extends the range of functions of the protein by attaching to it other biochemical functional groups such as acetate, phosphate, various lipids and carbohydrates, by changing the chemical nature of an amino acid e.g. Also, enzymes may remove amino acids from the amino end of the protein, or cut the peptide chain in the middle. acetylation, the addition of an acetyl group, usually at the N-terminus of the protein alkylation, the addition of an alkyl group e.g. biotinylation, acylation of conserved lysine residues with a biotin ...
*  Adaptor hypothesis
... The 'adaptor hypothesis' is part of a scheme to explain how information encoded in DNA is used to specify the amino acid sequence of proteins. It was formulated by Francis Crick in the mid-1950s, together with the central dogma of molecular biology and the sequence hypothesis. It first appeared in an informal publication of the RNA Tie Club in 1955 and was formally published in an article “On Protein Synthesis” in 1958. The adaptor hypothesis was framed to explain how information could be extracted from a nucleic acid and used to put together a string of amino acids in a specific sequence, that sequence being determined by the nucleotide sequence of the nucleic acid DNA or RNA template. Crick proposed that each amino acid is first attached to its own specific “adaptor” piece of nucleic acid in an enzyme-catalysed reaction. The order of assembly of the amino acids is then determined by a ...
*  internal peptide sequencing
... kraepiel kraepiel at Tue Aug 25 17:41:17 EST 1998. Previous message: Q: structure of protein complex + alanine scan Next message: Postdoctoral Position in Protein Expression and Purification Messages sorted by:. Some time ago there was a discussion about the best way to go about digesting a protein to obtain internal peptide sequence. Of course I was not paying attention then and now I need the information. I have a partially purified protein preparation and can with which I can get an isolated band of my protein of interest by SDS PAGE. If I electroelute this protein, digest it and run a gel to obtain isolated fragments I will probably lose a lot during these manipulations. This protein is pretty low copy number and it is difficult to get enough to sequnce. I would be grateful for any alternative strategies one might use to get internal sequence. Todd Lane Tlane at Previous message: Q: structure of protein complex + alanine scan Next message: Postdoctoral ...
*  Coiled coil
Folding a sequence with this repeating pattern into an alpha-helical secondary structure causes the hydrophobic residues to be presented as a 'stripe' that coils gently around the helix in left-handed fashion, forming an amphipathic structure. Upon binding of gp120 to the CD4 receptor and coreceptor, a number of conformational changes in the structure leads to the dissociation of gp120 and to the exposure of gp41 and at the same time to the anchoring of the gp41 N-terminal fusion peptide sequence into the host cell. HR1 forms a parallel, trimeric coiled coil onto which HR2 region coils, forming the trimer-of-hairpins or six-helix bundle structure, thereby facilitating membrane fusion through bringing the membranes close to each other. The general problem of deciding on the folded structure of a protein when given the amino acid sequence the so-called protein folding problem has not been solved. performed a landmark study using an archetypal coiled coil, GCN4, in which rules ...
'SOSUI' is a free online tool that predicts a part of the secondary structure of protein s from a given amino acid sequence AAS. The main objective is to determine whether the protein in question is a soluble or a transmembrane protein. History How SOSUI works Results Sources External links. First of all, SOSUI looks for α helices that are relatively easy to predict, taking into account the known helical potential s of the given amino acid sequence AAS. The much more difficult task is to differentiate between the α helices in soluble proteins and the ones in transmembrane proteins, the α helix being a very common secondary structure pattern in proteins. " hydropathy index " Kyte und Doolittle 1982 weighted presence of amphiphilic amino acids AA and their localization: "amphiphilicity index" the AA's charge the length of the AAS. An important improvement compared to Kyte und Doolittle's "hydropathy index", which relies entirely on one characteristic, is ...
*  NHL repeat
... infobox protein family symbol nhl name nhl repeat image pdb q f ebi jpg width caption structure of the brain tumor pumilio translation repressor complex pfam pf pfam clan cl interpro ipr smart prosite scop q f tcdb opm family opm protein pdb the nhl repeat named after ncl ht a and lin is an amino acid sequence found largely in a large number of eukaryotic and prokaryotic protein s for example the repeat is found in a variety of enzymes of the copper type ii ascorbate dependent monooxygenase family which catalyse the c terminus alpha amidation of biological peptides in many it occurs in tandem arrays for example in the ring finger beta box coiled coil rbcc eukaryotic growth regulators the brain tumor protein brat is one such growth regulator that contains a bladed nhl repeat beta propeller the nhl repeats are also found in serine threonine protein kinase stpk in diverse range of pathogenic bacteria these stpk are transmembrane receptors with an intracellular n terminal kinase domain ...
*  Sequence motif
Overview Motif Representation Motifs and consensus sequences. Discovery through evolutionary conservation. Pattern description notations. For example, many DNA binding protein s that have affinity for specific DNA binding site s bind DNA in only its double-helical form. This pattern may be written as ' N{P} {P} ' where N = Asn, P = Pro, S = Ser, T = Thr; {X} means any amino acid except X ; and. Motifs and consensus sequences. For this reason, two or more patterns are often associated with a single motif: the defining pattern, and various typical patterns. For example, the defining sequence for the IQ motif may be taken to be:. 3 Discovery through evolutionary conservation. Pattern description notations. there is an alphabet of single characters, each denoting a specific amino acid or a set of amino acids; a string of characters drawn from the alphabet denotes a sequence of the corresponding amino acids; any string of ...
*  Proteolysis
'''Proteolysis''' is the breakdown of protein s into smaller polypeptide s or amino acids. Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. Proteolysis and diseases Non-enzymatic proteolysis Laboratory applications Protease enzymes Venoms. This may involve removal of the N-terminal methionine , signal peptide , and/or the conversion of an inactive or non-functional protein to an active one. 1 Removal of N-terminal methionine. Some proteins and most eukaryotic polypeptide hormones are synthesized as a large precursor polypeptide known as polyprotein that require proteolytic cleavage into individual smaller polypeptide chains. In digestion of food, digestive enzymes may be released into the environment for extracellular digestion whereby proteolytic cleavage ...
*  Patente US6841377 - Human kinase and polynucleotides encoding the same - Google Patentes
The invention also encompasses a DNA vectors that contain any of the foregoing NHK coding sequences and/or their complements i.e., antisense ; b DNA expression vectors that contain any of the foregoing NHK coding sequences operatively associated with a regulatory element that directs the expression of the coding sequences for example, baculovirus as described in U.S. The NHK Sequences The cDNA sequences and the corresponding deduced amino acid sequence of the described NHK are presented in the Sequence Listing. USA 82:6148-6152 ; gene targeting in embryonic stem cells Thompson et al., 1989, Cell 56:313-321 ; electroporation of embryos Lo, 1983, Mol Cell. Such functionally equivalent NHK proteins include, but are not limited to, additions or substitutions of amino acid residues within the amino acid sequence encoded by the NHK nucleotide sequences described above, but which result in a silent change, thus ...
*  Primary structure of proteins
... redirect protein primary structure
*  actos time of day - MedHelp
... Actos time of day. Read More. I am tak I ng 850 mg of Metf or m I n tw I ce a I l I ght>day I l I ght>. Read More. I exper I enced th I s f or the f I rst I l I ght>t I me I l I ght> about 6 years ago. Read More. Read More. Read More. There I s I ncreas I ng ev I dence that th I s en do cr I ne abn or mal I ty can be reversed by treatment w I th w I dely ava I lable standard med I cat I ons wh I ch are lead I ng med I c I nes used I n th I s country f or the treatment of adult onset d I abetes, metf or m I n Glucophage 500 or 850 mg three t I mes per I l I ght>day I l I ght> or 1000mg tw I ce da I ly w I th meals, p I ogl I tazone I l I ght> actos I l I ght> 15-30 mg once a I l I ght>day I l I ght>, ros I gl I tazone Avand I a 4-8 mg once da I ly or a comb I nat I on of these med I cat I ons. Read More. Read More. I saw my do c the other I l I ght>day I l I ght>. Read More. 1 so I t went do wn but I know I ts gone back up because dur I ng the last month I 've gotten 300-400's and thats w I th tak I ng ...
*  N-end rule
n end rule n end rule the n end rule is a rule related to ubiquitination discovered by alexander varshavsky and co workers in the rule states that the n terminal amino acid of a protein determines its half life likelihood of being degraded the rule applies to both eukaryotic and prokaryotic organisms but with different strength however only rough estimations of protein half life can be deduced from this rule as n terminal amino acid modification can lead to variability and anomalies whilst amino acid impact can also change from organism to organism other degradation signals known as degron s can also be found in sequence relationships n terminal residues approximate half life of proteins for s cerevisiae met gly ala ser thr val pro hrs stabilizing ile glu approx min stabilizing tyr gln approx min destabilizing leu phe asp lys approx min destabilizing arg approx min destabilizing n terminal residues approximate half life of proteins in mammalian systems val h ...
*  ROSALIND | Translating RNA into Protein
ROSALIND. Translating RNA into Protein. About. Project. FAQ. Courses. Faculty. Problems. List View. Tree View. Topics. Add Problem. Statistics. Top 100. Countries. Levels. Badges. Achievements. Glossary. Log in. Register. It appears that your browser has JavaScript disabled. Rosalind requires your browser to be JavaScript enabled. Translating RNA into Protein. solved by 7933. July 2, 2012, midnight by Rosalind Team. The Genetic Code. Figure 1. The human hemoglobin molecule consists of 4 polypeptide chains; α subunits are shown in red and β subunits are shown in blue. Just as nucleic acids are polymers of nucleotides, proteins are chains of smaller molecules called amino acids ; 20 amino acids commonly appear in every species. Just as the primary structure of a nucleic acid is given by the order of its nucleotides, the primary structure of a protein is the order of its amino acids. Some proteins are composed of several subchains called polypeptides, ...
*  Getting ready for First peptide use. -
Getting ready for First peptide use. News. Supplement News. Nutrition News. Weight Loss News. Training News. Research News. Forum. Supplement Forum. Nutrition Forum. Weight Loss Forum. Training Forum. Main Forum. Supplement Forum. Nutrition Forum. Weight Loss Forum. Training Forum. Album Gallery. Forum. IGF-1/GH. Getting ready for First peptide use. Getting ready for First peptide use. Getting ready for First peptide use. I took this from a website Sunday - Off Training - Mid-day PegMGF 200-300mcg Monday - Training Afternoon Tuesday - Off Training - Afternoon IGF 80mcg Wednesday - Training Afternoon Thursday - Off Training - Afternoon IGF 80mcg Friday - Training Afternoon Saturday - Off Training - Afternoon IGF 80mcg Here is a excerpt from the article- In a natural system Our Body we have peaks and dips with MGF and IGF levels. The reasons for these peaks and dips are to create the ideal amount of cells to repair and create new tissue. After strenuous exercise the levels of MGF in the body more specifically ...
*  Lifson–Roig model
In polymer science, the 'Lifson–Roig model' is a helix-coil transition model applied to the alpha helix - random coil transition of polypeptide s;. 1 it is a refinement of the Zimm-Bragg model that recognizes that a polypeptide alpha helix is only stabilized by a hydrogen bond only once three consecutive residues have adopted the helical conformation. To consider three consecutive residues each with two states helix and coil, the Lifson–Roig model uses a 4x4 transfer matrix instead of the 2x2 transfer matrix of the Zimm-Bragg model, which considers only two consecutive residues. The Lifson–Roig model is characterized by three parameters: the statistical weight for nucleating a helix, the weight for propagating a helix and the weight for forming a hydrogen bond, which is granted only if three consecutive residues are in a helical state. Weights are assigned at each position in a polymer as a function of the conformation of the residue in that position and as a function of its two neighbors. 0 n 1 The ...–Roig_model
*  KCNQ1 - Potassium voltage-gated channel subfamily KQT member 1 - Homo sapiens (Human)
/p> p> a href='../manual/protein existence' target=' top'>More... /p> p> a href='../manual/function section' target=' top'>More... p>Manually curated information for which there is published experimental evidence. p>Manually curated information for which there is published experimental evidence. p>Manually curated information for which there is published experimental evidence. See also OMIM:192500 Feature key Position s Length Description Graphical view Feature identifier Actions p>Describes natural variant s of the protein sequence. Heart Rhythm 2:507-517 2005 Cited for : VARIANTS LQT1 71-ALA--PRO-73 DEL; THR-73; GLY-115; TYR-122; ILE-133; PHE-136; LYS-160; ARG-168; CYS-174; GLN-190; PHE-204; LEU-225; ASN-235; ASN-242; CYS-243; MET-254; 254-VAL--PHE-256 DEL; CYS-259; LEU-259; ASP-261; PRO-266; SER-269; ASP-269; PHE-273; ARG-273; SER-276 DEL; LEU-277; HIS-278; LYS-290; ASP-292; CYS-293; VAL-302; ARG-304; SER-305; ILE-312; SER-314; ARG-314; ASP-314; CYS-315; ARG-316; ALA-322; PHE-339 ...
* - Figure
www jbiol com figure resolution standard high figure schematic diagram of synonymous substitutions between human and murine hoxc and hoxb nucleotide sequences this diagram shows that many more synonymous substitutions blue bars are present in hoxb than in hoxc the two conserved elements ces identified in hoxc by lin et al are indicated as well as the position of the homeodomain hd the sliding window strategy is visualized by the positioning of a bp window within a ce as well as over the homeodomain which is not a ce because it does not contain stretches of consecutive bases devoid of synonymous substitutions the sequence encoding the homeodomain at the amino acid sequence level one of the most conserved features of hox genes still contains multiple synonymous substitutions in both hoxc and hoxb whereas the region of hoxc which encodes a domain of the protein without any clearly defined function is virtually conserved it should be noted that the hoxb protein is overall ...
* - Figure
... Resolution: standard / high Figure 2. Comparison of cells expressing the C-terminal domains of moesin, ezrin and radixin. NIH3T3 cells were transfected with C-terminal domain-GFP fusion proteins of ezrin and radixin As with moesin, no effect on cell behavior is seen 6 hours after transfection a,b Similar to C-moesin and consistent with identical amino acid sequences of the F-actin-binding region, both C-ezrin and C-radixin bind to actin filaments in stress fibers sf b,c,e,f and numerous microextensions. This localization is sensitive to cytochalasin D. Litman et al. BMC Cell Biology 2000 1 :1-1 doi:10.1186/1471-2121-1-1 Download authors' original image.
*  Organic Molecules - AP Biology Video by Brightstorm
5,934 views. Third, I'll go through the proteins, very important topic and finish off with the nucleic acids. Now these five carbon or six carbon sugars, can very often not only be in these what are called straight chains, but they can manoeuvre and join to form ring structures. So you could see glucose has a group of six carbons and a linear form or straight chain form, or forming this ring structure, the hexagon shape. Now, as a group, unfortunately the fats and lipids don't have a common monomer like the carbohydrates do with the monosaccharides or the proteins do with the amino acids. Let's take a look first at one of the two major groups which are the triglycerides and phospholipids and they will have a common structure that we can see here. And by doing that, we pull out a water, and now we've joined together our two amino acids. Again, because the old name of the amino acids was peptides, that's also why an amino acid ...
*  Patent US6130037 - Biosensor device and method - Google Patents
A biosensor apparatus for detecting a binding event between a ligand and ligand-binding receptor, comprising an electrode substrate having a detection surface, formed on said detection surface, a monolayer composed of hydrocarbon chains anchored at their proximal ends to the detection surface; also anchored to the detection surface, a heterodimer-subunit complex composed of first and second peptides that together form an -helical coiled-coil heterodimer, and said ligand, where i said first peptide is covalently bound to the detection surface, at surface sites distinct from those at which the-hydrocarbon chains are anchored, ii said ligand is covalently attached to the second peptide, iii said hydrocarbon chains are sufficiently close-packed and ordered such that binding of the second peptide to the first peptide, to form said heterodimer-subunit complex, is effective to measurably reduce the electron flow across the monolayer mediated by a redox ion species in an aqueous medium, relative to electron flow ...
* - Figure
www biomedcentral com figure resolution standard high figure effects of peptide length on recognition of vp peptides by antibodies raised against the first n terminal residues of ev vp the top panel shows the elisa reaction of the polyclonal serum to peptides truncated at the carboxyl end of the mer the bottom shows the same with the truncations at the amino end and the highlighted yellow region shows the minimal apparent core of the peptide for antibody recognition the plus signs on the right of the diagram illustrate whether the polyclonal serum binds to the peptide fragment od optical density at nm zhao et al bmc microbiology doi download authors original image
*  Endoproteinase Lys-C
endoproteinase lys c endoproteinase lys c endoproteinase lys c is a protease that cleaves proteins on the c terminal side of lysine amino acids lys c activity is optimal in ph range of references category peptidase category ec category posttranslational modification
* - Figure
www jbiol com figure resolution standard high figure unc is homologous to mammalian scoco a sequence alignment of unc scoco proteins from s cerevisiae c elegans c briggsae mosquito drosophila fugu zebrafish xenopus mouse and human residues identical in all ten sequences are shaded black similar residues are shaded gray the underlined region is predicted in all cases to form a coiled coil domain the region boxed in green is acidic and the region boxed in red is serine threonine rich the bracket indicates the carboxy terminal basic region asterisks mark mutations in unc b mrna of the human unc homolog scoco is enriched in fetal brain and is also present in fetal kidney liver and lung c expression of human scoco rescues the locomotion defect of unc mutant movement of the wild type wt mutants and transgenic l stage hermaphrodites was scored as complete sine waves per minute for each genotype n error bars represent the standard error of the mean su et al journal of biology doi jbiol download ...
*  Functions
... of Protein Now, let's take a quick look at the functions of proteins. There are quite a few different kinds of functions that proteins serve. There are structural proteins, such as muscle and hair. There are enzymes which control chemical reactions. There are also carrier proteins, such as hemoglobin and myoglobin that carry oxygen through the bloodstream and into the cells. Form and Function The molecular structure of proteins is very important in how the proteins carry out their functions. Proteins that are structural proteins have to be large. It's also very important that these be insoluble in water, and therefore, the side groups on the amino acids that are used are generally nonpolar side groups. On the other hand, for things like the enzymes and carriers and antibodies, these in comparison are quite a bit smaller, and in order to facilitate their mobility within the blood and cell fluids, it's necessary that these quite often have polar side groups to allow them to be more soluble. ...
* - Figure
... Resolution: standard / high Figure 9. Alignment of polypeptide sequences retrieved with motif 9 vs. N -terminal part of a large precursor of AM-1 toxins P69929. Mature polypeptides are shown in black, while signal peptides and propeptide domains are in light brown; amino acids in AV-toxins that differ from the sequence of AM-1 toxin precursor are given in red. Kozlov and Grishin BMC Genomics 2011 12 :88 doi:10.1186/1471-2164-12-88 Download authors' original image.
*  Interleukin 26
interleukin interleukin interleukin il is a protein that in humans is encoded by the il gene il is a amino acid protein which is similar in amino acid sequence to interleukin it was originally called ak and is composed of a signal sequence helices and conserved cysteine residues il is expressed in certain herpesvirus transformed t cells but not in primary stimulated t cells il signals through a receptor complex comprising two distinct proteins called il receptor and il receptor by signaling through this receptor complex il induces rapid phosphorylation of the transcription factors stat and stat which enhance il and il secretion and as expression of the cd molecule on the surface of epithelial cells references further reading
*  BMW 325 for sale: La Puente, CA - Listings
... Find a Dealer. Review a Dealer. Advanced Search Favorites: Saved Cars 0 Saved Searches 0. BMW 325s for sale 202 matches near La Puente, CA. Cars Dealers. Your Search Make BMW. Save Search Clear all. Ci 49. Get a fair-price estimate Find certified dealers nearby Read expert advice. Black, 4 door, RWD, Sedan, 6-Speed Automatic, 3.0L I6 24V MPFI DOHC, Stock# K41076LL. Black, 4 door, RWD, Sedan, 6-Speed Automatic, 3.0L I6 24V MPFI DOHC, Stock# 759. Black, 4 door, RWD, Sedan, 6-Speed Automatic, 3.0L I6 24V MPFI DOHC, Stock# 699. White, 4 door, RWD, Sedan, 6-Speed Automatic, 3.0L I6 24V MPFI DOHC, Stock# 738. Black, 4 door, RWD, Sedan, 6-Speed Automatic, 3.0L I6 24V MPFI DOHC, Stock# W6391. White, 2 door, RWD, Convertible, 5-Speed Automatic, 2.5L I6 24V MPFI DOHC, Stock# 15153. Black, 4 door, RWD, Sedan, 6-Speed Automatic, 3.0L I6 24V MPFI DOHC, Stock# T16148. Black, 4 door, RWD, Sedan, 6-Speed Automatic, 3.0L I6 24V MPFI DOHC, Stock# K38878. Blue, 4 door, RWD, Sedan, 5-Speed Automatic, 2.5L I6 24V MPFI DOHC, ...
*  Pfam: DUF342
... Database: Pfam Entry: DUF342 LinkDB: DUF342 Original site: DUF342. All links. No link information was found. #=GF ID DUF342 #=GF AC PF03961.9 #=GF DE Protein of unknown function DUF342 #=GF AU Bateman A #=GF SE COG1315 #=GF GA 32.40 32.40; #=GF TC 32.90 32.50; #=GF NC 32.20 31.80; #=GF BM hmmbuild HMM.ann SEED.ann #=GF SM hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq #=GF TP Family #=GF WK Domain of unknown function #=GF DR INTERPRO; IPR005646 ; #=GF CC This family of bacterial proteins has no known function. The #=GF CC proteins are in the region of 500-600 amino acid residues in #=GF CC length.
*  Fundamentals of Programming using C++ by Baldwin
fundamentals of programming using c by baldwin close the files listing invokes the close method on both of the file i o stream objects to flush the output buffers disassociate the stream objects from the two specific files etc so now you know how to read and write data from files in c and how to use that data in conjunction with arrays which is another requirement of the master syllabus for this course listing also signals the end of the dosomething function and the end of the lesson end
*  Alec Baldwin Has The Most Commercial Scifi Concept Ever
*  Al Fin: Mining Space--A Gold Rush that Never Ends
... 10 May 2007 Mining Space--A Gold Rush that Never Ends. In 2004, the world production of iron ore exceeded 1,000 million metric tons. In comparison, a comparatively small M-type asteroid with a mean diameter of 1 km could contain more than 2,000 million metric tons of iron-nickel ore, or two to three times the annual production for 2004. Who will benefit from the exploitation of space. Information on this area has made plain that the costs of initial start-up and initial maintenance are beyond the capability of the non industrialized nations and can only be undertaken by nations with large developed economic infrastructures, specifically the European Union, The U.S., possibly Russia and Japan. Each of these has positive and negative factors which will determine how large a share of space industry and mining they will control. Labels: Access to space, asteroids, mining, space exploration, space resources, space travel. posted by al fin at 8:25 AM. Great post. Although, as I argue on my blog, space travel ...
*  Family of proteins
... redirect protein family
*  Cheap and Free Domain Name Registration
... DEDICATED SERVERS When you want to smoke the competition, GlowHost Managed Dedicated Servers are how you get it done. Cheap and Free Domain Name Registration. Web Hosting Features Domain Name Registration. Cheap and Free Domain Name Registration Cheap Domain Registration from $1.99. Get your domain registration from as little as $1.99 when you order any non-domain product from our domain registration partner, FREE Domain Name Registration. More about free domain names ... GlowHost Domain Name Registration Services. Get your FREE Domain now. Why are you giving away free domain names. We believe that if you choose GlowHost as your web hosting provider, you will be so happy with the features and service that we provide, that you will have no reason to switch to another provider for your hosting and domain name needs. Learn more about free domain names. Bulk Domain Name Registration Bulk domain name registration is right for individuals who want to register 2 or more domains at a time. Bulk ...
*  A1 domain
a domain a domain redirect list of a genes proteins or receptors
*  Panasonic 14mm F2.5 review data at various sites.: Micro Four Thirds Talk Forum: Digital Photography
... Review. Reviews. Sample Images. Videos. Lenses. Forums. Forum index. Micro Four Thirds Talk Change forum Panasonic 14mm F2.5 review data at various sites. Shop cameras lenses ▾. Forum Parent First Previous Next Next unread. jericho77. Panasonic 14mm F2.5 review data at various sites. Aug 5, 2013. Reply to thread Reply with quote. Forum Parent First Previous Next Next unread. Posted by When Panasonic 14mm F2.5 review data at various sites. jericho77. Aug 5, 2013. Re: Panasonic 14mm F2.5 review data at various sites. Aug 5, 2013 3. Re: Panasonic 14mm F2.5 review data at various sites. Aug 5, 2013. Re: Panasonic 14mm F2.5 review data at various sites. Aug 5, 2013. Re: Panasonic 14mm F2.5 review data at various sites. jericho77. Aug 5, 2013. Aug 5, 2013. jericho77. Aug 5, 2013. Re: Panasonic 14mm F2.5 review data at various sites. jericho77. Aug 5, 2013. Re: Panasonic 14mm F2.5 review data at various sites. Aug 5, 2013 1. Re: Panasonic 14mm F2.5 review data at various sites. Alumna Gorp. Aug 5, 2013. ...
*  The genetic basis of a plant-insect coevolutionary key innovation. Proc Natl Acad Sci USA (PDF Downl
Proc Natl Acad Sci USA PDF Download Available. Proc Natl Acad Sci USA. © 2007 by The National Academy of Sciences of the USA fossil calibrated, Bayesian relaxed molecular clock estimation of the Pierinae–Coliadinae divergence. Fossil and molecular data agree that the Brassicales appeared by 90 to 85 Mya, which is much earlier than the parallel evolution of glucosinolates in the Euphorbiaceae 58 Mya 28. In this article, we directly address the timing of the appearance of the glucosinolate-feeding Pierinae, using several independent molecular datasets and various calibration methods to generate a robust estimate of when Pieridae evolved relative to their Brassicales host plants. Pieridae-specific temporal reconstruction used a Bayesian relaxed molecular clock method on EF-1. Current and expected diversity, and divergence estimates for the Coliadinae and Pierinae subfamilies of Pieridae. However, there are significantly more species of Pierinae than expected, ...
*  Mystery of bacterial growth and resistance solved: Findings shed light on how bacteria form protecti
... ve biofilms -- ScienceDaily. Your source for the latest research news. Mystery of bacterial growth and resistance solved: Findings shed light on how bacteria form protective biofilms. Date: April 26, 2012 Source: The Scripps Research Institute Summary: Scientists have unraveled a complex chemical pathway that enables bacteria to form clusters called biofilms. Scientists at The Scripps Research Institute have unraveled a complex chemical pathway that enables bacteria to form clusters called biofilms. Past research had also revealed that nitric oxide is involved in influencing bacterial biofilm formation. Nitric Oxide Modulates Bacterial Biofilm Formation through a Multicomponent Cyclic-di-GMP Signaling Network. The Scripps Research Institute. "Mystery of bacterial growth and resistance solved: Findings shed light on how bacteria form protective biofilms." ScienceDaily. The Scripps Research Institute. Mystery of bacterial growth and resistance solved: Findings shed light on how bacteria form protective ...
*  Mankin Lab - Publications
Browse by year: 2014    2013    2012    2011    2010    2009    2008    2007    2006    2005    2004    2003    2002    2001    2000    1999    1998    1997    1996    1995   . Proc Natl Acad Sci USA 111, 9804-9809. 2014 The general mode of translation inhibition by macrolide antibiotics Proc Natl Acad Sci USA 111, 15958–15963. Top. Top. Top. Proc Natl Acad Sci USA 108, 5931-5932. Proc Natl Acad Sci USA 108, 10496-10501. Vázquez-Laslop, N., Ramu, H., Mankin, A. 2011 Nascent peptide in the ribosome exit tunnel affects functional properties of the A-Site of the peptidyl transferase center Mol Cell 41, 321-330. Top. Proc Natl Acad Sci USA 107, 1983-1988. A., Xiong, L., Mankin, A. H D 2010 Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action Proc Natl Acad Sci USA 107, ...
*  GO:1900911 regulation of olefin biosynthetic process
... Services. Research. Training. Industry. About us. QuickGO A fast browser for Gene Ontology terms and annotations. EBI Databases QuickGO GO:1900911 regulation of olefin biosynthetic process. Search for terms by keyword or ID: apoptosis GO:0006915 Search for proteins by name or accession: tropomyosin P06727. Web Services. Dataset. Term Basket. Term Information ID GO:1900911. Name regulation of olefin biosynthetic process. Ontology Biological Process. Definition Any process that modulates the frequency, rate or extent of olefin biosynthetic process. GONUTS GO:1900911 Wiki Page. Synonyms. Synonyms are alternative words or phrases closely related in meaning to the term name, with indication of the relationship between the name and synonym given by the synonym scope. Click on the icon for more details. Type Synonym. exact regulation of olefin synthesis. exact regulation of olefin biosynthesis. exact regulation of olefin formation. exact regulation of olefin anabolism. Ancestor Chart This chart is interactive; ...
*  Albums by Smokey Robinson : Rhapsody
... JavaScript is disabled in your browser settings. requires JavaScript. Cancel. Free trial. x Music. Apps Devices. Pricing. Sign up. Company Info. Careers. Press Media. Partners. Account. Customer Support. Redeem Coupon. Buy a Gift. 2015 Rhapsody International Inc. ×. Rhapsody App for. Rhapsody International, Inc. Get app. Have the app. Music Apps Devices Pricing Listen Now Try Rhapsody. Sign In. Home. / Music. / Soul/R B. / Motown. / Smokey Robinson. / Facebook. Twitter. Albums by Smokey Robinson. Main Releases. Play. Smokey & Friends. Smokey Robinson. Play. Be Near Me. Smokey Robinson. Play. The Motown Years Live. Smokey Robinson. Play. Ev'ry Man Should Know. Smokey Robinson. Play. The Solo Anthology. Smokey Robinson. Play. The Stripped Mixes. Smokey Robinson. Play. Time Flies When You're Having Fun. Smokey Robinson. Play. Love Songs. Smokey Robinson. Play. Timeless Love. Smokey Robinson. Play. The Definitive Collection. Smokey Robinson. Play. 20th Century Masters: The Millennium ...

Protein primary structure: The primary structure of a peptide or protein is the linear sequence of its amino acid structural units, and partly comprises its overall biomolecular structure. By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end.Coles PhillipsLigation-independent cloning: Ligation-independent cloning (LIC) is a form of molecular cloning that is able to be performed without the use of restriction endonucleases or DNA ligase. This allows genes that have restriction sites to be cloned without worry of chopping up the insert.Proteinogenic amino acid: Proteinogenic amino acids are amino acids that are precursors to proteins, and are incorporated into proteins cotranslationally — that is, during translation. There are 23 proteinogenic amino acids in prokaryotes (including N-Formylmethionine, mainly used to initiate protein synthesis and often removed afterward), but only 21 are encoded by the nuclear genes of eukaryotes.Symmetry element: A symmetry element is a point of reference about which symmetry operations can take place. In particular, symmetry elements can be centers of inversion, axes of rotation and mirror planes.CS-BLASTList of strains of Escherichia coli: Escherichia coli is a well studied bacterium that was first identified by Theodor Escherich, after whom it was later named.Molar mass distribution: In linear polymers the individual polymer chains rarely have exactly the same degree of polymerization and molar mass, and there is always a distribution around an average value. The molar mass distribution (or molecular weight distribution) in a polymer describes the relationship between the number of moles of each polymer species (Ni) and the molar mass (Mi) of that species.DNA condensation: DNA condensation refers to the process of compacting DNA molecules in vitro or in vivo. Mechanistic details of DNA packing are essential for its functioning in the process of gene regulation in living systems.Branching order of bacterial phyla (Gupta, 2001): There are several models of the Branching order of bacterial phyla, one of these was proposed in 2001 by Gupta based on conserved indels or protein, termed "protein signatures", an alternative approach to molecular phylogeny. Some problematic exceptions and conflicts are present to these conserved indels, however, they are in agreement with several groupings of classes and phyla.DNA binding site: DNA binding sites are a type of binding site found in DNA where other molecules may bind. DNA binding sites are distinct from other binding sites in that (1) they are part of a DNA sequence (e.DNA sequencer: A DNA sequencer is a scientific instrument used to automate the DNA sequencing process. Given a sample of DNA, a DNA sequencer is used to determine the order of the four bases: G (guanine), C (cytosine), A (adenine) and T (thymine).Database of protein conformational diversity: The Database of protein conformational diversity (PCDB) is a database of diversity of protein tertiary structures within protein domains as determined by X-ray crystallography. Proteins are inherently flexible and this database collects information on this subject for use in molecular research.Ferric uptake regulator family: In molecular biology, the ferric uptake regulator (FUR) family of proteins includes metal ion uptake regulator proteins. These are responsible for controlling the intracellular concentration of iron in many bacteria.Margaret Jope: Margaret Jope (1913–2004) was a Scottish biochemist, born as Henrietta Margaret Halliday in Peterhead, Scotland.Specificity constant: In the field of biochemistry, the specificity constant (also called kinetic efficiency or k_{cat}/K_{M}), is a measure of how efficiently an enzyme converts substrates into products. A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.Mature messenger RNA: Mature messenger RNA, often abbreviated as mature mRNA is a eukaryotic RNA transcript that has been spliced and processed and is ready for translation in the course of protein synthesis. Unlike the eukaryotic RNA immediately after transcription known as precursor messenger RNA, it consists exclusively of exons, with all introns removed.High-performance liquid chromatography: High-performance liquid chromatography (HPLC; formerly referred to as high-pressure liquid chromatography), is a technique in analytical chemistry used to separate, identify, and quantify each component in a mixture. It relies on pumps to pass a pressurized liquid solvent containing the sample mixture through a column filled with a solid adsorbent material.Silent mutation: Silent mutations are mutations in DNA that do not significantly alter the phenotype of the organism in which they occur. Silent mutations can occur in non-coding regions (outside of genes or within introns), or they may occur within exons.SEA Native Peptide LigationBurst kinetics: Burst kinetics is a form of enzyme kinetics that refers to an initial high velocity of enzymatic turnover when adding enzyme to substrate. This initial period of high velocity product formation is referred to as the "Burst Phase".Open reading frame: In molecular genetics, an open reading frame (ORF) is the part of a reading frame that has the potential to code for a protein or peptide. An ORF is a continuous stretch of codons that do not contain a stop codon (usually UAA, UAG or UGA).Triparental mating: Triparental mating is a form of Bacterial conjugation where a conjugative plasmid present in one bacterial strain assists the transfer of a mobilizable plasmid present in a second bacterial strain into a third bacterial strain. Plasmids are introduced into bacteria for such purposes as transformation, cloning, or transposon mutagenesis.Short linear motifEssential amino acid: An essential amino acid or indispensable amino acid is an amino acid that cannot be synthesized de novo (from scratch) by the organism, but must be supplied in its diet. The nine amino acids humans cannot synthesize are phenylalanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysine, and histidine (i.Reaction coordinateChymotrypsinHeterodimeric amino-acid transporter: Heterodimeric amino-acid transporters are a family of transport proteins that facilitate the transport of certain amino acids across cell membranes. Each transporter comprises a two-protein, a light and heavy, subunit.Library (biology): In molecular biology, a library is a collection of DNA fragments that is stored and propagated in a population of micro-organisms through the process of molecular cloning. There are different types of DNA libraries, including cDNA libraries (formed from reverse-transcribed RNA), genomic libraries (formed from genomic DNA) and randomized mutant libraries (formed by de novo gene synthesis where alternative nucleotides or codons are incorporated).Beef cattle: Beef cattle are cattle raised for meat production (as distinguished from dairy cattle, used for milk production). The meat of adult cattle is known as beef.Ethyl groupFERM domain: In molecular biology, the FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane.Codon Adaptation Index: The Codon Adaptation Index (CAI) is the most widespread technique for analyzing Codon usage bias. As opposed to other measures of codon usage bias, such as the 'effective number of codons' (Nc), which measure deviation from a uniform bias (null hypothesis), CAI measures the deviation of a given protein coding gene sequence with respect to a reference set of genes.Thermal cyclerLattice protein: Lattice proteins are highly simplified computer models of proteins which are used to investigate protein folding.Proximity ligation assay: Proximity ligation assay (in situ PLA) is a technology that extends the capabilities of traditional immunoassays to include direct detection of proteins, protein interactions and modifications with high specificity and sensitivity. Protein targets can be readily detected and localized with single molecule resolution and objectively quantified in unmodified cells and tissues.Transmembrane domain: Transmembrane segment usually denotes a single transmembrane alpha helix of a transmembrane protein, also known as an integral protein.http://www.Size-exclusion chromatography: Size-exclusion chromatography (SEC) is a chromatographic method in which molecules in solution are separated by their size, and in some cases molecular weight. It is usually applied to large molecules or macromolecular complexes such as proteins and industrial polymers.TEV protease: TEV protease (also called Tobacco Etch Virus nuclear-inclusion-a endopeptidase) is a highly sequence-specific cysteine protease from Tobacco Etch Virus (TEV). It is a member of the PA clan of chymotrypsin-like proteases.Protein subcellular localization prediction: Protein subcellular localization prediction (or just protein localization prediction) involves the computational prediction of where a protein resides in a cell.Eukaryotic transcription: Eukaryotic transcription is the elaborate process that eukaryotic cells use to copy genetic information stored in DNA into units of RNA replica. Gene transcription occurs in both eukaryotic and prokaryotic cells.ParaHox: The ParaHox gene cluster is an array of homeobox genes (involved in morphogenesis, the regulation of patterns of anatomical development) from the Gsx, Xlox (Pdx) and Cdx gene families.New Zealand rabbitChicken as biological research model: Chickens (Gallus gallus domesticus) and their eggs have been used extensively as research models throughout the history of biology. Today they continue to serve as an important model for normal human biology as well as pathological disease processes.Translational regulation: Translational regulation refers to the control of the levels of protein synthesized from its mRNA. The corresponding mechanisms are primarily targeted on the control of ribosome recruitment on the initiation codon, but can also involve modulation of the elongation or termination of protein synthesis.Zuotin: Z-DNA binding protein 1, also known as Zuotin, is a Saccharomyces cerevisiae yeast gene.ThermolysinProlyl endopeptidase: Prolyl endopeptidase (PE) also known as prolyl oligopeptidase or post-proline cleaving enzyme is an enzyme that in humans is encoded by the PREP gene.Restriction fragment: A restriction fragment is a DNA fragment resulting from the cutting of a DNA strand by a restriction enzyme (restriction endonucleases), a process called restriction. Each restriction enzyme is highly specific, recognising a particular short DNA sequence, or restriction site, and cutting both DNA strands at specific points within this site.LeucineMembrane protein: Membrane proteins are proteins that interact with biological membranes. They are one of the common types of protein along with soluble globular proteins, fibrous proteins, and disordered proteins.Biopterin-dependent aromatic amino acid hydroxylase: In molecular biology, the biopterin-dependent aromatic amino acid hydroxylases (abbreviated AAAH) constitute a family of aromatic amino acid hydroxylases, including phenylalanine 4-hydroxylase (), tyrosine 3-hydroxylase (), and tryptophan 5-hydroxylase (). These enzymes primarily hydroxylate phenylalanine, tyrosine, and tryptophan, respectively.Allele-specific oligonucleotide: An allele-specific oligonucleotide (ASO) is a short piece of synthetic DNA complementary to the sequence of a variable target DNA. It acts as a probe for the presence of the target in a Southern blot assay or, more commonly, in the simpler Dot blot assay.Cryptic self epitopes: In immunology, cryptic self epitopes are a source of autoimmunity.KonzoGating signal: A gating signal is a digital signal or pulse (sometimes called a "trigger") that provides a time window so that a particular event or signal from among many will be selected and others will be eliminated or discarded.Molecular evolution: Molecular evolution is a change in the sequence composition of cellular molecules such as DNA, RNA, and proteins across generations. The field of molecular evolution uses principles of evolutionary biology and population genetics to explain patterns in these changes.Chromosome regionsSubtherapeutic antibiotic use in swine: Antibiotics are commonly used in commercial swine production in the United States and around the world. They are used for disease treatment, disease prevention and control, and growth promotion.Liver sinusoid: A liver sinusoid is a type of sinusoidal blood vessel (with fenestrated, discontinuous endothelium) that serves as a location for the oxygen-rich blood from the hepatic artery and the nutrient-rich blood from the portal vein.SIU SOM Histology GI

(1/190738) The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. The tryptic peptides.

The NADP-specific glutamate dehydrogenase of Neurospora crassa was digested with trypsin, and peptides accounting for 441 out of the 452 residues of the polypeptide chain were isolated and substantially sequenced. Additional experimental detail has been deposited as Supplementary Publication SUP 50052 (11 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem J. (1975) 145, 5.  (+info)

(2/190738) The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptides from digestion with a staphylococcal proteinase.

The extracellular proteinase of Staphylococcus aureus strain V8 was used to digest the NADP-specific glutamate dehydrogenase of Neurospora crassa. Of 35 non-overlapping peptides expected from the glutamate content of the polypeptide chain, 29 were isolated and substantially sequenced. The sequences obtained were valuable in providing overlaps for the alignment of about two-thirds of the sequences found in tryptic peptides [Wootton, J. C., Taylor, J, G., Jackson, A. A., Chambers, G. K. & Fincham, J. R. S. (1975) Biochem. J. 149, 739-748]. The blocked N-terminal peptide of the protein was isolated. This peptide was sequenced by mass spectrometry, and found to have N-terminal N-acetylserine by Howard R. Morris and Anne Dell, whose results are presented as an Appendix to the main paper. The staphylococcal proteinase showed very high specificity for glutamyl bonds in the NH4HCO3 buffer used. Partial splits of two aspartyl bonds, both Asp-Ile, were probably attributable to the proteinase. No cleavage of glutaminyl or S-carboxymethylcysteinyl bonds was found. Additional experimental detail has been deposited as Supplementary Publication SUP 50053 (5 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K, from whom copies may be obtained under the terms given in Biochem. J. (1975) 1458 5.  (+info)

(3/190738) Novel regulation of the homeotic gene Scr associated with a crustacean leg-to-maxilliped appendage transformation.

Homeotic genes are known to be involved in patterning morphological structures along the antero-posterior axis of insects and vertebrates. Because of their important roles in development, changes in the function and expression patterns of homeotic genes may have played a major role in the evolution of different body plans. For example, it has been proposed that during the evolution of several crustacean lineages, changes in the expression patterns of the homeotic genes Ultrabithorax and abdominal-A have played a role in transformation of the anterior thoracic appendages into mouthparts termed maxillipeds. This homeotic-like transformation is recapitulated at the late stages of the direct embryonic development of the crustacean Porcellio scaber (Oniscidea, Isopoda). Interestingly, this morphological change is associated with apparent novelties both in the transcriptional and post-transcriptional regulation of the Porcellio scaber ortholog of the Drosophila homeotic gene, Sex combs reduced (Scr). Specifically, we find that Scr mRNA is present in the second maxillary segment and the first pair of thoracic legs (T1) in early embryos, whereas protein accumulates only in the second maxillae. In later stages, however, high levels of SCR appear in the T1 legs, which correlates temporally with the transformation of these appendages into maxillipeds. Our observations provide further insight into the process of the homeotic leg-to-maxilliped transformation in the evolution of crustaceans and suggest a novel regulatory mechanism for this process in this group of arthropods.  (+info)

(4/190738) The Drosophila kismet gene is related to chromatin-remodeling factors and is required for both segmentation and segment identity.

The Drosophila kismet gene was identified in a screen for dominant suppressors of Polycomb, a repressor of homeotic genes. Here we show that kismet mutations suppress the Polycomb mutant phenotype by blocking the ectopic transcription of homeotic genes. Loss of zygotic kismet function causes homeotic transformations similar to those associated with loss-of-function mutations in the homeotic genes Sex combs reduced and Abdominal-B. kismet is also required for proper larval body segmentation. Loss of maternal kismet function causes segmentation defects similar to those caused by mutations in the pair-rule gene even-skipped. The kismet gene encodes several large nuclear proteins that are ubiquitously expressed along the anterior-posterior axis. The Kismet proteins contain a domain conserved in the trithorax group protein Brahma and related chromatin-remodeling factors, providing further evidence that alterations in chromatin structure are required to maintain the spatially restricted patterns of homeotic gene transcription.  (+info)

(5/190738) The homeobox gene Pitx2: mediator of asymmetric left-right signaling in vertebrate heart and gut looping.

Left-right asymmetry in vertebrates is controlled by activities emanating from the left lateral plate. How these signals get transmitted to the forming organs is not known. A candidate mediator in mouse, frog and zebrafish embryos is the homeobox gene Pitx2. It is asymmetrically expressed in the left lateral plate mesoderm, tubular heart and early gut tube. Localized Pitx2 expression continues when these organs undergo asymmetric looping morphogenesis. Ectopic expression of Xnr1 in the right lateral plate induces Pitx2 transcription in Xenopus. Misexpression of Pitx2 affects situs and morphology of organs. These experiments suggest a role for Pitx2 in promoting looping of the linear heart and gut.  (+info)

(6/190738) Mrj encodes a DnaJ-related co-chaperone that is essential for murine placental development.

We have identified a novel gene in a gene trap screen that encodes a protein related to the DnaJ co-chaperone in E. coli. The gene, named Mrj (mammalian relative of DnaJ) was expressed throughout development in both the embryo and placenta. Within the placenta, expression was particularly high in trophoblast giant cells but moderate levels were also observed in trophoblast cells of the chorion at embryonic day 8.5, and later in the labyrinth which arises from the attachment of the chorion to the allantois (a process called chorioallantoic fusion). Insertion of the ROSAbetageo gene trap vector into the Mrj gene created a null allele. Homozygous Mrj mutants died at mid-gestation due to a failure of chorioallantoic fusion at embryonic day 8.5, which precluded formation of the mature placenta. At embryonic day 8.5, the chorion in mutants was morphologically normal and expressed the cell adhesion molecule beta4 integrin that is known to be required for chorioallantoic fusion. However, expression of the chorionic trophoblast-specific transcription factor genes Err2 and Gcm1 was significantly reduced. The mutants showed no abnormal phenotypes in other trophoblast cell types or in the embryo proper. This study indicates a previously unsuspected role for chaperone proteins in placental development and represents the first genetic analysis of DnaJ-related protein function in higher eukaryotes. Based on a survey of EST databases representing different mouse tissues and embryonic stages, there are 40 or more DnaJ-related genes in mammals. In addition to Mrj, at least two of these genes are also expressed in the developing mouse placenta. The specificity of the developmental defect in Mrj mutants suggests that each of these genes may have unique tissue and cellular activities.  (+info)

(7/190738) A Drosophila doublesex-related gene, terra, is involved in somitogenesis in vertebrates.

The Drosophila doublesex (dsx) gene encodes a transcription factor that mediates sex determination. We describe the characterization of a novel zebrafish zinc-finger gene, terra, which contains a DNA binding domain similar to that of the Drosophila dsx gene. However, unlike dsx, terra is transiently expressed in the presomitic mesoderm and newly formed somites. Expression of terra in presomitic mesoderm is restricted to cells that lack expression of MyoD. In vivo, terra expression is reduced by hedgehog but enhanced by BMP signals. Overexpression of terra induces rapid apoptosis both in vitro and in vivo, suggesting that a tight regulation of terra expression is required during embryogenesis. Terra has both human and mouse homologs and is specifically expressed in mouse somites. Taken together, our findings suggest that terra is a highly conserved protein that plays specific roles in early somitogenesis of vertebrates.  (+info)

(8/190738) Requirement of a novel gene, Xin, in cardiac morphogenesis.

A novel gene, Xin, from chick (cXin) and mouse (mXin) embryonic hearts, may be required for cardiac morphogenesis and looping. Both cloned cDNAs have a single open reading frame, encoding proteins with 2,562 and 1,677 amino acids for cXin and mXin, respectively. The derived amino acid sequences share 46% similarity. The overall domain structures of the predicted cXin and mXin proteins, including proline-rich regions, 16 amino acid repeats, DNA-binding domains, SH3-binding motifs and nuclear localization signals, are highly conserved. Northern blot analyses detect a single message of 8.9 and 5.8 kilo base (kb) from both cardiac and skeletal muscle of chick and mouse, respectively. In situ hybridization reveals that the cXin gene is specifically expressed in cardiac progenitor cells of chick embryos as early as stage 8, prior to heart tube formation. cXin continues to be expressed in the myocardium of developing hearts. By stage 15, cXin expression is also detected in the myotomes of developing somites. Immunofluorescence microscopy reveals that the mXin protein is colocalized with N-cadherin and connexin-43 in the intercalated discs of adult mouse hearts. Incubation of stage 6 chick embryos with cXin antisense oligonucleotides results in abnormal cardiac morphogenesis and an alteration of cardiac looping. The myocardium of the affected hearts becomes thickened and tends to form multiple invaginations into the heart cavity. This abnormal cellular process may account in part for the abnormal looping. cXin expression can be induced by bone morphogenetic protein (BMP) in explants of anterior medial mesoendoderm from stage 6 chick embryos, a tissue that is normally non-cardiogenic. This induction occurs following the BMP-mediated induction of two cardiac-restricted transcription factors, Nkx2.5 and MEF2C. Furthermore, either MEF2C or Nkx2.5 can transactivate a luciferase reporter driven by the mXin promoter in mouse fibroblasts. These results suggest that Xin may participate in a BMP-Nkx2.5-MEF2C pathway to control cardiac morphogenesis and looping.  (+info)


  • In mammals, the UGTs are membrane-bound proteins of approximately 530 amino acid residues residing in the endoplasmic reticulum. (
  • Our results show that by simply exchanging two amino acid residues, we could modulate the divalent cation requirement in the uridylylation of GlnJ and GlnB. (
  • Do the amino acid sequence identities of residues that make contact across protein interfaces covary during evolution? (
  • This is a membrane-permeable phosphoducin-like anti-βγ peptide, whose membrane-permeable sequence (MPS) is derived from the C-terminal residues of phosducin-like protein (PhLP). (
  • 3. Chains of optimal length close the ends by interactions between two amino acid residues. (
  • The amino-acid sequence of acutobin contains a single chain of 236 residues including four potential N-glycosylation sites. (


  • Two maltose binding protein fusion proteins, 2B7F1 and 2B7F2, incorporating the first 157 or 119 amino acids, respectively, of UGT2B7 were expressed in Escherichia coli and purified by affinity chromatography. (
  • We find that residue pairs identified using a pseudo-likelihood based method to covary across protein-protein interfaces in the 50S ribosomal unit and 28 additional bacterial protein complexes with known structure are almost always in contact in the complex provided that the number of aligned sequences is greater than the average of the lengths of the two proteins. (
  • These proteins (or certain domains) are unfolded and yet are perfectly functional, and in many cases are just as highly conserved as folded protein domains, though often of lower sequence complexity [1] (and hence, easier to evolve via random generation). (
  • Despite the practically unlimited number of possible protein sequences, the number of basic shapes in which proteins fold seems not only to be finite, but also to be relatively small, with probably no more than 10,000 folds in existence. (


  • Their functions are encoded in a linear sequence of amino acids, of which only 20 species are found in nature. (
  • Extensive screening of the venom gland cDNA species after amplification by PCR resulted in the isolation of four distinct cDNA clones encoding acutobin and three other serine proteases, designated Dav-PA, Dav-KN and Dav-X. The complete amino acid sequences of these enzymes were deduced from the cDNA sequences. (
  • The phylogenetic tree of the complete amino acid sequences of 40 serine proteases from 18 species of Crotalinae shows functional clusters reflecting parallel evolution of the three major venom enzyme subtypes: coagulating enzymes, kininogenases and plasminogen activators. (


  • Activity studies of expressed chimeric UGT cDNAs have shown that the aglycone binding domain is likely to be seated within the first 298 amino acids of the N terminus of the protein, presumably in the region amino acids 55 to 180, a region with least homology of primary sequence between the UGT isoforms ( Mackenzie, 1990 ). (
  • The PhLP shares amino acid sequence homology with phosphoducin, a phosphoprotein expressed in the retina and pineal gland. (


  • Each fasta file begins with the T. thermophilus amino acid sequence pair, with other homologous sequences trimmed to match its length. (
  • In some cases of RNA virus recombination, the donor sequence neatly replaces a homologous region of the acceptor sequence leaving its structure unchanged. (
  • hybrid sequences resulting from aberrant homologous recombination (when similar viruses exchange sequence without maintaining strict alignment) and nonhomologous recombination (recombination between unrelated RNA sequences) are also commonly observed (Lai, 1992). (


  • Sequence similarities Belongs to the G-protein coupled receptor 1 family. (
  • Sequence similarities Belongs to the chaperonin (HSP60) family. (
  • Sequence similarities Belongs to the phosphatase 2A regulatory subunit B56 family. (

protein sequences

  • An alignment of the Erm protein sequences. (
  • ASR entails the prediction of ancient DNA and protein sequences based on information from extant sequences 8 . (


  • Phylogenetic analysis of 17 putative ABC transporters from the isolated strains with 23 reference sequences of ABC transporters described in actinobacteria. (
  • In the isolates, distances of erm gene sequences were significantly correlated to phylogenetic distances based on 16S rRNA genes, while ABC transporter gene distances were not. (


  • Comparative evolutionary studies provide detailed information about DNA sequence and mRNA expression differences between humans and other primates but, in the absence of other information, it has proved very difficult to identify molecular pathways relevant to human cognition. (
  • Using available genomic sequence data on coagulation factor VIII and predictive models of molecular evolution, we engineer protein variants with improved activity, stability. (


  • The full-length cDNA sequence of CcPrx4 consisted of 884 nucleotides with an open reading frame encoding a mature protein of 247 amino acids. (
  • Partial sequences were completed by performing 5′ RACE with the Marathon cDNA Amplification kit (Clontech, Palo Alto, CA) according to the manufacturer's protocol with Marathon-Ready cDNA from human fetal brain (Clontech) as a template. (


  • An alignment of partial 16S rRNA gene sequences of the isolated strains examined in the study. (
  • An alignment of amino-acid ABC transporter sequences. (
  • An alignment of 16S rRNA gene sequences. (
  • Sequence alignment of TodS like sensor kinases. (


  • If there were a mutation in a ribosome that prevented tRNA molecules from moving into the E site, how many amino acids would be found in the resulting peptide chain formed on this ribosome? (
  • The inability to sufficiently 'humanize' ortholog-hybrid molecules with xenogeneic sequences, similarly to what is done for monoclonal antibody biologics, is a major limitation of ortholog-scanning for pharmaceutical development. (


  • However, the combinatorial complexity associated with identifying the multiple, non-linear amino acid determinants blocked further humanization. (

gene sequence

  • In principle, this approach can be applied to any protein drug based on a conserved gene sequence. (
  • First, we brie¯y review current knowledge of RNA virus recombination and describe new methods for detecting its occurrence using gene sequence data. (


  • This ortholog-scanning approach led to the creation of a highly expressed human/porcine hybrid FVIII named ET3 with 149 (11%) porcine amino acids. (


  • To find such genes, we expanded the sequence of the most differentially expressed novel TEM s and used hydrophobicity plots to predict cell surface localization. (
  • In contrast to ortholog scanning, it provides a higher-resolution mapping through comparisons of sequential phylogeny branches, and infers novel sequences with high potential for intended biomolecular functions as they are predicted to have once existed. (


  • Approximately 80% of its protein sequence was determined by sequencing the various fragments derived from CNBr cleavage and digestion with endoprotease. (


  • However, in the analysis of sequences from genomes where both resistance genes occurred together the correlation was observed for both ABC transporter and erm genes in actinobacteria but in streptomycetes only in the erm gene. (
  • We then identified and determined the sequence of the mouse counterparts of these genes and used in situ hybridization to examine mRNA expression patterns in murine tumors, embryos, and adult tissues. (


  • In this study, we demonstrate that the opioid binding site in UGT2B7 is within the first 119 amino-terminal amino acids. (
  • Morphine was found to bind at a single site within the first 119 amino acids and to undergo a conformational change upon binding, as demonstrated by transferred nuclear Overhauser effect spectroscopy. (
  • Conclusions: The type of erm resistance gene sequences was influenced by linkage to 16S rRNA gene sequences and site characteristics. (
  • We concluded that the amino acids at positions 42 and 85 in GlnJ and GlnB (in the vicinity of the ATP binding site) influence the divalent cation requirement for uridylylation catalyzed by GlnD. (


  • Their high rates of mutation and replication allow them to move through sequence space at a pace that often makes their DNA-based hosts ' evolution look glacial by comparison. (


  • Multiple sequence alignments used in the Ribosome 50S analysis. (
  • Multiple sequence alignments used in E. coli gene pair analysis. (


  • Ten single nucleotide polymorphisms in the SFTPC sequence were found in IPF patients and not in controls. (


  • A second process, recombination, can occur ineither segmented or unsegmented viruses when `donor'nucleotide sequence is introduced into a single, contiguous ` acceptor ' RNA molecule to produce a new RNA containing genetic information from more than one source. (


  • Mutations that change the amino acid sequence of a polypeptide often result in the production of a defective protein. (
  • Only one of these created an exonic change resulting in a change in amino acid sequence. (
  • In this case, a T to C substitution resulted in a change in amino acid 73 of the precursor protein from isoleucine to threonine. (


  • When amino acids are joined together to form a polypeptide chain, a waste molecule is given off as a result of this chemical reaction. (


  • Multiple sequence alignments used for the PDB benchmark set. (


  • At about the same time, Nozaki and Tanford's (1971) studies of amino acid hydrophobicity and Tanford's (1973) classic book on the hydrophobic effect stimulated critical investigations of the partitioning of amino acid side chains into nonpolar phases. (


  • When you break the hormone apart to study its structure, you find that it is composed of many amino acids. (

What is the human insulin amino acid sequence?

  • Okay, I'm doing a Biology project that involves finding the sequence of the human insulin amino acid sequence. Although I've googled it many times, all of the websites don't tell me what I need to know. If any of you don't know what I'm talking about, It's the sequence of codons that looks like: GCA-TCG-AAT-CGG-ACG-TTT-CAA, and so fourth. If you have an answer, please tell me or give me a website, thanks.
  • Have you tried this source ? Nature 187, 483 - 485 (06 August 1960); doi:10.1038/187483a0 Amino-Acid Sequence of Human Insulin D. S. H. W. NICOL* & L. F. SMITH†

What is the difference between glutamine and amino acid pills?

  • Having read maximuscle's workout plan it says to take amino acid tablets in workout but reading descriptions of glutamine pills it says glutamine is an there a difference or do i have to buy both pills to see optimum workout recovery
  • there are 20 different amino acids glutamine is one of them so id imagine that "amino acid pills" contain a mixture of amino acids, perhaps including glutamine

How many amino acid pills should i take before and after workout?

  • How many amino acid pills should i take before and after workout?
  • it depends on the dosage recomended if its 4 then 2 before and 2 after but instead of the amino acid pills i would take a drink called EXTEND you drink half before and half during the workout.. the only thing is u have to carry it with you in the shake container while u train

Is there a difference between an amino acid test based on saliva and one based on blood?

  • I have recently heard good things about a blood spot amino acid test that tests for your deficiancies and based on the outcome you can get supplements you need. My naturopath suggested an amino acid test based on saliva and I want to know if one is more accurate or better than the other?
  • Hi purplepansy. Cute 'name'. Amino acid imbalances are common and can cause significant health problems. Getting tested, therefore, may be a very good idea. Unfortunately, because I am not aware of the saliva test your doctor is recommending, I can't give you any advice on that. Ask your doctor this question. I am sure he/she will be happy to answer your concerns and provide you with documentation about the test's accuracy, reliability, etc. If you are really in doubt, have BOTH tests done. Serum amino acid profiles are valid and would provide a good comparison for the saliva test. If the results are similar, then you can do future/followup testing with the saliva method. Best wishes and good luck. P.S. I just received the results for my own serum amino acid profile yesterday. I get mine tested (along with many other tests) annually. I use Metamatrix Labs and their ION profile.

How do amino acids work when they're in diet pills?

  • I found these amino acid pills in the cupboard today and the bottle said they were diet supplements. How do they work as diet supplements? Like do they make you eat less or are they like laxatives? Also is 4 1000 (I don't know if it's mg or what) tablets too much? Because the bottle said to take 4 a day. It also says it's a balanced blend of 20 amino acids. So what does this all mean?
  • Diet supplements" are different from "Diet Pills" Supplements are vitamins, essentially. They are taken to supplement (replace) the vitamins, or in this case, amino acids, that you may not be getting in your day-to-day diet (not meaning to lose weight, just meaning what you eat) Diet pills are (a hoax) supposed to help decrease appetite, make you poop, less water retention etc... they don't work though. Sorry. Now to answer your question about aminos... Below is a list of some of the ways that amino acids have been used. Arginine - has been shown to improve sperm count and sperm motility in some men. Lysine - is used particularly for recurrent cold sores and herpes infections. Phenylalanine - has been used in the treatment of pain and depression. Tryptophan - this amino acid has been more studied than the others. There is an association between the level of tryptophan in the blood and arthritis. High levels of tryptophan are also found in jaundice. It has also been used in depression, particularly if insomnia is present. Oestrogen containing oral contraceptives interfere with the normal metabolism of tryptophan (this may be because of their effect in vitamin B6 which is essential for the conversion of tryptophan to serotonin.) Histidine - has been used in rheumatoid arthritis - low levels of histidine has been found in the blood of those with rheumatoid arthritis Tyrosine - like tryptophan and phenylalanine has been used in the treatment of depression. This amino acid is essential for the synthesis of substances called catecholamines (these include dopamine and noradrenaline) and some people who are depressed have low levels of these compounds. It is likely that more and more uses for amino acids will become evident as research progresses. Proteins (which contain amino acids) are essential requirement in our diet. Amino acids, essential and non-essential, are needed for the body's structural component - bones, muscle and connective tissue and for functional aspects such as hormones and other chemicals. The range of therapeutic used for which amino acids are used is still somewhat limited it is likely that the uses will expand as we learn more about the role that amino acids play in maintaining health.

What amino acid must I combine with "oat groats" to make to make them a complete protein?

  • I understand that the oat groats contain a higher quality and quantity of protein than most other grains, but they still lack an amino acid(s) to make them a compete protein. Quinoa is the only "so-called" grain that contains all the branched chain amino acids, but it actually is more related to a vegetable like spinach.
  • Check out this link and site. It gives you the amino acid profile of every food, and if an amino acid is missing (in this case I believe it's lysine & tryptophan) you can click on a link to find complementing amino acids.

I was wondering what's the difference between the amino acid and protein shakes?

  • I've been lifting for around 3 months now inorder to gaine muscel mass for my rowing practice.Im dowing fine still i need to gaine at least 20lp of muscel,so i'll start taking protein shakes or amino acid separately in my diet but i need to know which is better and what the difference.
  • Protein and Amino acid are both needed for muscle growth, BUT... The use of protein and amino acid supplements by athletes just isn't needed. Most athletes, including vegetarians, can easily get all the protein they need through a healthy diet. There isn't any good scientific evidence that shows that the addition of protein or amino acid supplements to a good diet based on the Food Guide Pyramid will increase muscle strength or size, enhance endurance, or decrease body fat, These goals can be obtained only through a well-thought-out training program coupled with a healthy diet.

How important are amino acids in weight lifting?

  • I am looking to gain muscle mass and gain weight. I take supplements like whey, creatine and NO and i was just wondering how important amino acids are in order to acheive my goal of gaining weight and muscle mass. Basicly im wondering whether or not to buy amino acid capsules along and add them with the other supplements i take. Thanks
  • Exactly as stated before - Proteins are made of chains of amino acids. Our bodies break down foreign proteins into Amino Acids and use them to build the proteins that make up our lean body mass. So giving your body Amino Acids just takes out the breaking down step that your body has to do. What I would suggest is that you take Optimum Nutrition (ON) whey protein which has BCAA's (a type of amino acid) in its formula already as your whey supplement. I wouldn't worry about the capsules. Plus any stand alone Amino Acids taste horrible. BTW I love Gaspari Nutrition products, they have helped me yield significant gains. You should look them up. Super pump 250 + Size On