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.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.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.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.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, 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.Amino Acid Transport Systems: Cellular proteins and protein complexes that transport amino acids across biological membranes.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.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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.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.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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.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.Amino Acids, Aromatic: Amino acids containing an aromatic side chain.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.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.Amino Acids, Branched-Chain: Amino acids which have a branched carbon chain.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Amino Acids, SulfurKinetics: The rate dynamics in chemical or physical systems.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Leucine: An essential branched-chain amino acid important for hemoglobin formation.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).Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.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.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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.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).Molecular Weight: The sum of the weight of all the atoms in a molecule.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.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.Bacterial Proteins: Proteins found in any species of bacterium.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.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.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.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.Genes, Bacterial: The functional hereditary units of BACTERIA.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.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.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.Amino Acid Transport Systems, Basic: Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).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.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.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.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.Amino Acids, Basic: Amino acids with side chains that are positively charged at physiological pH.Lysine: An essential amino acid. It is often added to animal feed.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.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.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.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.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).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.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 3.4.21.4.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.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.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.Amino Acids, DiaminoGlutamine: 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.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).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.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.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.Excitatory Amino Acids: Endogenous amino acids released by neurons as excitatory neurotransmitters. Glutamic acid is the most common excitatory neurotransmitter in the brain. Aspartic acid has been regarded as an excitatory transmitter for many years, but the extent of its role as a transmitter is unclear.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Arginine: An essential amino acid that is physiologically active in the L-form.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.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.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.Sequence Deletion: Deletion of sequences of nucleic acids from the genetic material of an individual.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.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.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.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.Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.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.Mutagenesis: Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.Amino Acid Transport System A: A sodium-dependent neutral amino acid transporter that accounts for most of the sodium-dependent neutral amino acid uptake by mammalian cells. The preferred substrates for this transporter system include ALANINE; SERINE; and GLUTAMINE.Amino Acids, Neutral: Amino acids with uncharged R groups or side chains.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.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.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.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.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.DNA, Bacterial: Deoxyribonucleic acid that makes up the genetic material of bacteria.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.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.Evolution, Molecular: The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.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.Viral Proteins: Proteins found in any species of virus.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.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.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.Receptors, Amino Acid: Cell surface proteins that bind amino acids and trigger changes which influence the behavior of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and GAMMA-AMINOBUTYRIC ACID and glycine receptors are the most common receptors for fast inhibition.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.Epitopes: Sites on an antigen that interact with specific antibodies.Dietary Proteins: Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.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).Protein PrecursorsCOS 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).)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.Protein Sorting Signals: Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.Amino Acids, Cyclic: A class of amino acids characterized by a closed ring structure.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.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.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.Repetitive Sequences, Amino Acid: A sequential pattern of amino acids occurring more than once in the same protein sequence.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.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.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.Aminoisobutyric Acids: A group of compounds that are derivatives of the amino acid 2-amino-2-methylpropanoic acid.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.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.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.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)Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Peptide 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.Amino Acyl-tRNA Synthetases: A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.Fungal Proteins: Proteins found in any species of fungus.DNA Mutational Analysis: Biochemical identification of mutational changes in a nucleotide sequence.Glutamic Acid: A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.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.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.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Carbon Isotopes: Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.Chromosome Mapping: Any method used for determining the location of and relative distances between genes on a chromosome.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)Large Neutral Amino Acid-Transporter 1: A CD98 antigen light chain that when heterodimerized with CD98 antigen heavy chain (ANTIGENS, CD98 HEAVY CHAIN) forms a protein that mediates sodium-independent L-type amino acid transport.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.Genetic Variation: Genotypic differences observed among individuals in a population.Oligopeptides: Peptides composed of between two and twelve amino acids.Genes, Fungal: The functional hereditary units of FUNGI.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)Tyrosine: A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.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.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.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.Cystine: A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.Amino Acids, Acidic: Amino acids with side chains that are negatively charged at physiological pH.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.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.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.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.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).Asparagine: A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd 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.Magnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.Culture Media: Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.Caseins: A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.Stereoisomerism: The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Mutation, Missense: A mutation in which a codon is mutated to one directing the incorporation of a different amino acid. This substitution may result in an inactive or unstable product. (From A Dictionary of Genetics, King & Stansfield, 5th ed)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.Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.Cercopithecus aethiops: A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.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.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Genes, Viral: The functional hereditary units of VIRUSES.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.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.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.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)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.HeLa Cells: The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.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)Histidine: An essential amino acid that is required for the production of HISTAMINE.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.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.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)CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.Xenopus laevis: The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Transaminases: A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.Cationic Amino Acid Transporter 1: A high-affinity, low capacity system y+ amino acid transporter found ubiquitously. It has specificity for the transport of ARGININE; LYSINE; and ORNITHINE. It may also act as an ecotropic leukemia retroviral receptor.Amino Acid Isomerases: Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.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.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.Protein Engineering: Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.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 Transport Proteins: Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS.Dipeptides: Peptides composed of two amino acid units.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Carboxypeptidases: Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.Glucose: A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Biological Transport, Active: The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.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)Biological Evolution: The process of cumulative change over successive generations through which organisms acquire their distinguishing morphological and physiological characteristics.

Covalent cross-linking of proteins without chemical reagents. (1/67)

A facile method for the formation of zero-length covalent cross-links between protein molecules in the lyophilized state without the use of chemical reagents has been developed. The cross-linking process is performed by simply sealing lyophilized protein under vacuum in a glass vessel and heating at 85 degrees C for 24 h. Under these conditions, approximately one-third of the total protein present becomes cross-linked, and dimer is the major product. Chemical and mass spectroscopic evidence obtained shows that zero-length cross-links are formed as a result of the condensation of interacting ammonium and carboxylate groups to form amide bonds between adjacent molecules. For the protein examined in the most detail, RNase A, the cross-linked dimer has only one amide cross-link and retains the enzymatic activity of the monomer. The in vacuo cross-linking procedure appears to be general in its applicability because five different proteins tested gave substantial cross-linking, and co-lyophilization of lysozyme and RNase A also gave a heterogeneous covalently cross-linked dimer.  (+info)

Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli. (2/67)

ClpB is a member of a multichaperone system in Escherichia coli (with DnaK, DnaJ, and GrpE) that reactivates strongly aggregated proteins. The sequence of ClpB contains two ATP-binding domains, each containing Walker consensus motifs. The N- and C-terminal sequence regions of ClpB do not contain known functional motifs. In this study, we performed site-directed mutagenesis of selected charged residues within the Walker A motifs (Lys212 and Lys611) and the C-terminal region of ClpB (Asp797, Arg815, Arg819, and Glu826). We found that the mutations K212T, K611T, D797A, R815A, R819A, and E826A did not significantly affect the secondary structure of ClpB. The mutation of the N-terminal ATP-binding site (K212T), but not of the C-terminal ATP-binding site (K611T), and two mutations within the C-terminal domain (R815A and R819A) inhibited the self-association of ClpB in the absence of nucleotides. The defects in self-association of these mutants were also observed in the presence of ATP and ADP. The four mutants K212T, K611T, R815A, and R819A showed an inhibition of chaperone activity, which correlated with their low ATPase activity in the presence of casein. Our results indicate that positively charged amino acids that are located along the intersubunit interface (this includes Lys212 in the Walker A motif of the N-terminal ATP-binding domain as well as Arg815 and Arg819 in the C-terminal domain) participate in intersubunit salt bridges and stabilize the ClpB oligomer. Interestingly, we have identified a conserved residue within the C-terminal domain (Arg819) which does not participate directly in nucleotide binding but is essential for the chaperone activity of ClpB.  (+info)

Both acidic and basic amino acids in an amphitropic enzyme, CTP:phosphocholine cytidylyltransferase, dictate its selectivity for anionic membranes. (3/67)

Amphitropic proteins are regulated by reversible membrane interaction. Anionic phospholipids generally promote membrane binding of such proteins via electrostatics between the negatively charged lipid headgroups and clusters of basic groups on the proteins. In this study of one amphitropic protein, a cytidylyltransferase (CT) that regulates phosphatidylcholine synthesis, we found that substitution of lysines to glutamine along both interfacial strips of the membrane-binding amphipathic helix eliminated electrostatic binding. Unexpectedly, three glutamates also participate in the selectivity for anionic membrane surfaces. These glutamates become protonated in the low pH milieu at the surface of anionic, but not zwitterionic membranes, increasing protein positive charge and hydrophobicity. The binding and insertion into lipid vesicles of a synthetic peptide containing the three glutamates was pH-dependent with an apparent pK(a) that varied with anionic lipid content. Glutamate to glutamine substitution eliminated the pH dependence of the membrane interaction, and reduced anionic membrane selectivity of both the peptide and the whole CT enzyme examined in cells. Thus anionic lipids, working via surface-localized pH effects, can promote membrane binding by modifying protein charge and hydrophobicity, and this novel mechanism contributes to the membrane selectivity of CT in vivo.  (+info)

The Est1 subunit of Saccharomyces cerevisiae telomerase makes multiple contributions to telomere length maintenance. (4/67)

The telomerase-associated Est1 protein of Saccharomyces cerevisiae mediates enzyme access by bridging the interaction between the catalytic core of telomerase and the telomere-binding protein Cdc13. In addition to recruiting telomerase, Est1 may act as a positive regulator of telomerase once the enzyme has been brought to the telomere, as previously suggested by the inability of a Cdc13-Est2 fusion protein to promote extensive telomere elongation in an est1-Delta strain. We report here three classes of mutant Est1 proteins that retain association with the telomerase enzyme but confer different in vivo consequences. Class 1 mutants display a telomere replication defect but are capable of promoting extensive telomere elongation in the presence of a Cdc13-Est2 fusion protein, consistent with a defect in telomerase recruitment. Class 2 mutants fail to elongate telomeres even in the presence of the Cdc13-Est2 fusion, which is the phenotype predicted for a defect in the proposed second regulatory function of EST1. A third class of mutants impairs an activity of Est1 that is potentially required for the Ku-mediated pathway of telomere length maintenance. The isolation of mutations that perturb separate functions of Est1 demonstrates that a telomerase holoenzyme subunit can contribute multiple regulatory roles to telomere length maintenance.  (+info)

Mutation of charged residues in the TR3 death domain does not perturb interaction with TRADD. (5/67)

Members of the death receptor family play a prominent role in developmental and pathological neuronal cell death. The death signal is transduced via interaction between the death domain of the receptor and an intracellular adapter, TRADD. We performed alanine-scanning mutagenesis of specific charged residues in the TR3 death domain to determine whether they play a crucial role in TR3-TR3 and TR3-TRADD interaction. Mutation of charged residues in the second and third helices of the TR3 death domain failed to perturb self-interaction or interaction with TRADD. These data suggest that despite some similarity between the death domains of TR3 and TNFR1 the nature of the interaction with TRADD differs from that reported for TNFR1.  (+info)

Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2. (6/67)

Rabphilin, Rim, and Noc2 have generally been believed to be the Rab3 isoform (Rab3A/B/C/D)-specific effectors that regulate secretory vesicle exocytosis in neurons and in some endocrine cells. The results of recent genetic analysis of rabphilin knock-out animals, however, strongly refute this notion, because there are no obvious genetic interactions between Rab3 and rabphilin in nematoda (Staunton, J., Ganetzky, B., and Nonet, M. L. (2001) J. Neurosci. 21, 9255-9264), suggesting that Rab3 is not a major ligand of rabphilin in vivo. In this study, I tested the interaction of rabphilin, Rim1, Rim2, and Noc2 with 42 different Rab proteins by cotransfection assay and found differences in rabphilin, Rim1, Rim2, and Noc2 binding to several Rab proteins that belong to the Rab functional group III (Rab3A/B/C/D, Rab26, Rab27A/B, and Rab37) and/or VIII (Rab8A and Rab10). Rim1 interacts with Rab3A/B/C/D, Rab10, Rab26, and Rab37; Rim2 interacts with Rab3A/B/C/D and Rab8A; and rabphilin and Noc2 interact with Rab3A/B/C/D, Rab8A, and Rab27A/B. By contrast, the synaptotagmin-like protein homology domain of Slp homologue lacking C2 domains-a (Slac2-a)/melanophilin specifically recognizes Rab27A/B but not other Rabs. I also found that alternative splicing events in the first alpha-helical region (alpha(1)) of the Rab binding domain of Rim1 alter the Rab binding specificity of Rim1. Site-directed mutagenesis and chimeric analyses of Rim2 and Slac2-a indicate that the acidic cluster (Glu-50, Glu-51, and Glu-52) in the alpha(1) region of the Rab binding domain of Rim2, which is not conserved in the synaptotagmin-like pro tein homology domain of Slac2-a, is a critical determinant of Rab3A recognition. Based on these results, I propose that Rim, rabphilin, and Noc2 function differently in concert with functional group III and/or VIII Rab proteins, including Rab3 isoforms.  (+info)

A PAR domain transcription factor is involved in the expression from a hematopoietic-specific promoter for the human LMO2 gene. (7/67)

The transcription factor LMO2 is believed to exert its effect through the formation of protein-protein interactions with other DNA-binding factors such as GATA-1 and TAL1. Although LMO2 has been shown to be critical for the formation of the erythroid cell lineage, the gene is also expressed in a number of nonerythroid tissues. In this report, we demonstrate that the more distal of the 2 promoters for the LMO2 gene is highly restricted in its pattern of expression, directing the hematopoietic-specific expression of this gene. Deletion and mutation analyses have identified a critical cis element in the first untranslated exon of the gene. This element is a consensus-binding site for a small family of basic leucine zipper proteins containing a proline and acidic amino acid-rich (PAR) domain. Although all 3 members of this family are produced in erythroid cells, only 2 of these proteins, thyrotroph embryonic factor and hepatic leukemia factor, can activate transcription from this LMO2 promoter element. These findings represent a novel mechanism in erythroid gene regulation because PAR proteins have not previously been implicated in this process.  (+info)

Close pairs of carboxylates: a possibility of multicenter hydrogen bonds in proteins. (8/67)

Covalent attachment of hydrogen to the donor atom may be not an essential characteristic of stable hydrogen bonds. A positively charged particle (such as a proton), located between the two negatively charged residues, may lead to a stable interaction of the two negative residues. This paper analyzes close Asp-Glu pairs of residues in a large set of protein chains; 840 such pairs of residues were identified, of which 28% were stabilized by a metal ion, 12% by a positive residue nearby and 60% are likely to be stabilized by a proton. The absence of apparent structural constraints, secondary structure preferences, somewhat lower B-factors and a distinct correlation between pH and the minimal O-O distance in carboxylate pairs suggest that most of the abnormally close pairs could indeed be stabilized by a shared proton. Implications for protein stability and modeling are discussed.  (+info)

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Glutamic acid Name L-Glutamic acid Molecular Weight 147.12926 g/mol Molecular Formula XLogP -3.3 CAS No. 56-86-0m.p.205℃pK1(25℃)2.10pK2(25℃)9.47pKR(25℃)4.07 Links * Amino acid * Acidic amino acid * Aspartic acid * Glutamic acid *
Determination of the molecular mass of M.EcoP1I by size-exclusion chromatography under nondenaturing conditions. (a) The standard curve Ve/Vo versus log molecul
Here, the mechanism of action of an antioxidant peptide rich in acidic amino acid residues in controlling lipid oxidation is discussed. Firstly, in the presence of this peptide, the fluorescence intensity of lipid peroxide in samples of walnut oil was very low, indicating that the peptide prevented the formation of lipid peroxides. Secondly, the production of lipid-derived radicals of oil was redu ...
The algal PIPs show many similarities with the PIPs of land plants and it is tempting to make the assumption that PIPs, with those shared features, were present already some 1000 MYA at the split of the chlorophytes and the streptophytes [10-12]. Land plant PIPs are known to be regulated by pH, Ca2+ and phosphorylation and a molecular gating mechanism has been suggested. In this, several of the residues have overlapping functions in controlling the D-loop conformation in response to the different signals. However, the evolution of the gating mechanism is likely to have been a stepwise process, starting out from a primitive regulatory mechanism and then sequentially adding further functionality. The presence of an among all PIPs conserved histidine crucial for pH gating [H193 in SoPIP2;1; 20, 21] in the algal PIPs, implies that this regulatory feature might be such a primitive mechanism. Contrary to this, the acidic amino acid residues responsible for Ca2+ binding (D28 and E31 in SoPIP2;1) are ...
Here, the mechanism of action of an antioxidant peptide rich in acidic amino acid residues in controlling lipid oxidation is discussed. Firstly, in the presence of this peptide, the fluorescence intensity of lipid peroxide in samples of walnut oil was very low, indicating that the peptide prevented the formation of lipid peroxides. Secondly, the production of lipid-derived radicals of oil was redu ...
The effects of excitatory amino acids on 22Na efflux rate in rat hippocampal slices were determined at various postnatal days and following removal of a major afferent system. Two weeks after a unilateral hippocampal aspiration, the 22Na efflux induc
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This report provides a guide to the development and presentation of 2014-2016 NSDUH substate estimates. A summary of the estimation methodology is included as well as sample sizes, response rates, and population estimates. This shapefile includes geographic boundaries of the 2014-2016 NSDUH substate regions along with prevalence rates, map group.... ...
This report provides a guide to the development and presentation of 2014-2016 NSDUH substate estimates. A summary of the estimation methodology is included as well as sample sizes, response rates, and population estimates. This shapefile includes geographic boundaries of the 2014-2016 NSDUH substate regions along with prevalence rates, map group.... ...
The protein encoded by this gene is an aminopeptidase which prefers acidic amino acids, and specifically favors aspartic acid over glutamic acid. It is thought to be a cytosolic protein involved in general metabolism of intracellular proteins. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2016 ...
What are zinc supplement health benefits are also such that you can increase it by having dairy products, eating wholegrain foods, lentils, pulses. Also even pumpkin is a very good source of zinc. Also zinc lozenges are easily available in drug stores which are mostly taken if you have cough or cold. What are zinc supplement health benefits is not a question to worry now so let me tell you what is the daily dose recommended for each person to be taken. For adults and teenage males it os preferred to be 9-12mg, pregnant women is to be 15mg, children from 1-10 years 3-9mg, and infants are preferred to take 2-3mg. So What are zinc supplement health benefits is now true. Also while seeing What are zinc supplement health benefits let me tell you that excess of anything is always harmful now this can be just anything. So excess of zinc in our body can prove to be fatal as it is toxic and reduces the function of iron and the iron levels in our body. So relating to What are zinc supplement health ...
I know that there are polar uncharged amino acids (serine, threonine, asparagine, glutamine, cysteine) and polar charged amino acids (the basic and acidic amino acids). Does the charge on the acidic and basic amino acids make them more polar and hydrophilic than the uncharged polar amino acids? Moreover, cysteine is classified as an uncharged amino acid, but because it has an ionizable side chain, would it be more polar than serine, asparagine, etc.? ...
A conserved substitution (K385R) did not affect either the apparent glycine EC50 (40 ± 1 versus 41 ± 0.5 μM) or the ethanol-induced potentiation (53 ± 5 versus 46 ± 5%) of the human α1 GlyR. On the other hand, replacement of this residue with glutamic acid (K385E), an acidic amino acid, reduced the potentiation of the GlyR to 10 ± 1%. Furthermore, mutations with a hydrophobic leucine (K385L), a hydrogen bond donor glutamine (K385Q), or a neutral residue (K385A) also reduced ethanol modulation. ...
May catalyze the decarboxylation of aspartate, cysteine sulfinic acid, and cysteic acid to beta-alanine, hypotaurine and taurine, respectively. Does not exhibit any decarboxylation activity toward glutamate.
植物 miRNA 與 mRNA 完全或接近完全的配對結合後, 會引起目標基因在配對的第十位核酸上發生剪切,進行基因表達的調控。 伴隨第二代定序的進步,利用 PARE* (Parallel Analysis of RNA Ends) 方法, 以降解組定序(Degradome Sequencing)測出剪切位點, 被剪切的 3 片段以 RNA 連接酶連接上 5 adaptor 後, 經反轉錄形成雙股 cDNA, 再以 EcoP 15I** 酵素切位接上 3 adaptor 後往下進行定序分析。 目前此方法已成功應用於阿拉伯芥,水稻等植物的降解組定序上 ...
Eukaryotic cells contain a huge variety of internally specialized subcellular compartments. Stoichiogenomics aims to reveal patterns of elements usage in biological macromolecules. However, the stoichiogenomic characteristics and how they adapt to various subcellular microenvironments are still unknown. Here we first updated the definition of stoichiogenomics. Then we applied it to subcellular research, and detected distinctive nitrogen content of nuclear and hydrogen, sulfur content of extracellular proteomes. Specially, we found that acidic amino acids (AAs) content of cytoskeletal proteins is the highest. The increased charged AAs are mainly caused by the eukaryotic originated cytoskeletal proteins. Functional subdivision of the cytoskeleton showed that activation, binding/association, and complexes are the three largest functional categories. Electrostatic interaction analysis showed an increased electrostatic interaction between both primary sequences and PPI interfaces of 3D structures, in the
Electrophoresis Package 1/8 is needed but not provided. __________________________________________________________. Here is a sample of the Student Manual:. IND-24 (Part A). Identifying Unknowns by Electrophoresis. Background Information. Many different types of biological molecules are charged at neutral pH as shown in the table below. For example, four of the twenty amino acids found in proteins are charged. The basic amino acids lysine and arginine carry a positive charge while the acidic amino acids aspartate and glutamate carry a negative one. Likewise synthetic dyes, which are similar in size to amino acids, are often acidic or basic. These dyes are commonly used to stain tissue sections, as food coloring agents and for coloring fabrics in the clothing industry. Proteins are composed of amino acids and thus basic proteins are generally rich in lysine and arginine and deficient in aspartate and glutamate while the reverse is true for acidic proteins. DNA and RNA molecules always carry a ...
Amino acids nonpolar polar basic acidic Stop codon Standard genetic code 1st. base 2nd base ... amino acid sequences and DNA sequences. Proteins with the same three-dimensional structure need not have identical amino acid ... that code redundantly for the same amino acid. Since many species use the same codon at the same place to specify an amino acid ... Had the amino acid sequences come from different ancestors, they would have been coded for by any of the redundant codons, and ...
Interaction of DNA (in orange) with histones (in blue). These proteins' basic amino acids bind to the acidic phosphate groups ... These encode the twenty standard amino acids, giving most amino acids more than one possible codon. There are also three 'stop ... Deoxyribonucleic acid (/diːˈɒksɪˌraɪboʊnjuːˌkliːɪk, -ˌkleɪ-/ (. listen);[1] DNA) is a molecule composed of two chains that coil ... Koltsov proposed that a cell's genetic information was encoded in a long chain of amino acids. See: *. Кольцов, Н. К. (12 ...
Conditioners are frequently acidic, as low pH protonates the keratin's amino acids. The hydrogen ions gives the hair a positive ... The surface of keratin contains negatively charged amino acids. Hair conditioners therefore usually contain cationic ... The surfactants are based on long, straight aliphatic fatty acid chains similar to saturated fatty acids. Their molecules have ... Organic acids such as citric acid are usually used to maintain acidity. ...
137 amino acids), acidic protein. As shown, J chain joins two µ chains via disulfide bonds involving cysteines in the ... also approximately 110 amino acids long). The µ heavy chain of IgM is a protein of ~576 amino acids, and includes a variable ... 220 amino acids, composed of a variable domain, VL (a segment of approximately 110 amino acids), and a constant domain, CL ( ... 110 amino acids), four distinct constant region domains (Cµ1, Cµ2, Cµ3, Cµ4, each ~110 amino acids) and a "tailpiece" of ~20 ...
Examples of zwitterions include amino acids, many metabolites, peptides, and proteins. Usually, non-dissolved salts at standard ... those that hydrolyze to produce hydronium ions in water are acidic salts. Neutral salts are those salts that are neither acidic ... nitric acid) Nitrite NO− 2 (nitrous acid) Oxide O2− Phosphate PO3− 4 (phosphoric acid) Sulfate SO2− 4 (sulfuric acid) Salts are ... carbonic acid) Chloride Cl− (hydrochloric acid) Citrate HOC(COO− )(CH 2COO− ) 2 (citric acid) Cyanide C≡N− (hydrocyanic acid) ...
In the case of acidic amino acids (e.g. aspartic acid) or basic amino acids (e.g. lysine), the pKa values of the two similar ... An amino acid contains both acidic (carboxylic acid fragment) and basic (amine fragment) centres. The isomer on the right is a ... the side chain and the amino group can both take a positive charge at low pH values, and in the case of amino acids with acidic ... The acid dissociation constants are defined as: K. a. 1. =. c. (. H. 3. O. +. ). ⋅. c. (. Zwitterion. ). c. (. Cation. ). K. a ...
The gene encodes a 336 amino acid acidic glycoprotein. It carries the antigenic determinants of the Duffy blood group system ... Fy-a and Fy-b differ by in a single amino acid at position 42: glycine in Fy-a and aspartic acid in Fy-b (guanine in Fy-a and ... The mouse ortholog has been cloned and exhibits 63% homology to the human gene at the amino acid level. The mouse gene is ... consisting of the amino acid substitution of arginine for a cysteine at position 89 of the protein diminishes the ability to ...
Human talin-1 is 270.0 kDa molecular weight and 2541 amino acids.[7] The N-terminal region of talin-1 is ~50 kDa in size and ... Talin-1 N-terminal region also binds acidic phospholipids for insertion into lipid bilayers.[17][18][19] The rod domain (,200 ... "A fluorescence cell biology approach to map the second integrin-binding site of talin to a 130-amino acid sequence within the ...
It is an odorless, white crystalline powder that is derived from the two amino acids aspartic acid and phenylalanine. It is ... It is more stable in somewhat acidic conditions, such as in soft drinks. Though it does not have a bitter aftertaste like ... When eaten, aspartame is metabolized into its original amino acids. Because it is so intensely sweet, relatively little of it ... When cooked or stored at high temperatures, aspartame breaks down into its constituent amino acids. This makes aspartame ...
Its conformation is retained mainly by disulfide bonds, as virtually all cysteine amino acids are found in the disulfide form, ... Hyalin is a large, acidic protein which aids in embryonic development. The protein has strong adhesive properties which can ... Within its sequence is a region containing tandem repeats of about 84 amino acids. This sequence is highly conserved between ... It encodes for approximately 25% acidic residues with only 3.5% basic residues. ...
Overall, the protein is composed mainly of charged amino acids, both acidic and basic. There were no regions of sustained non- ... It also comes in a second isoform that is 156 amino acids long. The gene contains a G-patch domain and the DUF 4138 domain. The ... In addition, it is low in amino acids such as valine, threonine, phenylalanine, and proline. It is a soluble protein and has a ... GPATCH11 has a molecular weight of about 33.3 kdal and is 285 amino acids long. ...
Aspartic acid (aspartate) is one of the most common amino acids in the typical diet. As with methanol and phenylalanine, intake ... Under strongly acidic or alkaline conditions, aspartame may generate methanol by hydrolysis. Under more severe conditions, the ... Aspartame is a methyl ester of the dipeptide of the natural amino acids L-aspartic acid and L-phenylalanine. ... In a study done in 1979, the effect of aspartame ingestion on blood and milk amino acid levels in lactating women was tested. ...
... and showed amino acid features common to all three. The role of neutral and acidic amino acids was shown for the first time in ... two clusters of basic amino acids, separated by a spacer of about 10 amino acids. Both signals are recognized by importin α. ... "Comparative mutagenesis of nuclear localisation signals reveals the importance of neutral and acidic amino acids". Curr. Biol. ... This PY-NLS motif, so named because of the proline-tyrosine amino acid pairing in it, allows the protein to bind to Importin β2 ...
Many cyanobacterial plastocyanins have 107 amino acids. Although the acidic patches are not conserved in bacteria the ... The protein is a monomer, with a molecular weight around 10,500 Daltons, and 99 amino acids in most vascular plants. It is a ... These hydrophobic and acidic patches are believed to be the recognition/binding sites for the other proteins involved in ... In plant plastocyanins, acidic residues are located on either side of the highly conserved tyrosine-83. Algal plastocyanins, ...
This extreme acidity is achieved by its amino acid sequence. Many portions of its chain are repeating -D-S-S- (aspartic acid- ... Phosphophoryn is the most acidic protein ever discovered and has an isoelectric point of 1. ...
A short stretch of acidic amino acids located between the D1 and D2 domains has auto-inhibitory functions. This 'acid box' ... "acidic fibroblast growth factor" (FGF1) and "basic fibroblast growth factor" (FGF2). These proteins had a high degree of amino ... complete amino acid sequence and homologies". Science. 230 (4732): 1385-8. Bibcode:1985Sci...230.1385G. doi:10.1126/science. ... These proteins were found to be identical to the acidic and basic FGFs described by Gospodarowicz, et al. FGFs are ...
... and amino acid composition. For example, tropomyosin is an acidic protein that migrates abnormally on SDS-PAGE gels. This is ... Nucleic acid molecules are separated by applying an electric field to move the negatively charged molecules through a matrix of ... Nucleic acids are often denatured by including urea in the buffer, while proteins are denatured using sodium dodecyl sulfate, ... The most common being, for nucleic acids Tris/Acetate/EDTA (TAE), Tris/Borate/EDTA (TBE). Many other buffers have been proposed ...
The high ratio of basic to acidic amino acids contributes to the protein's higher isoelectric point. C16orf95 is predicted to ... C16orf95 has a large number of amino acid changes over time, indicating it is a quickly evolving protein. There are no proteins ... The longest isoform of the C16orf95 protein has 239 amino acids. It has a conserved domain of unknown function spanning ...
It contains 374 amino acid residues. Its N-terminus is highly acidic and starts with an acetyled aspartate in its amino group. ... an analysis based on the amino acid sequence of the amino-terminal tryptic peptide". Journal of Molecular Biology. 126 (4): 783 ... Its amino acid sequence is also one of the most highly conserved of the proteins as it has changed little over the course of ... The amino acid sequencing of actin was completed by M. Elzinga and co-workers in 1973. The crystal structure of G-actin was ...
The protein it encodes for is 344 amino acids in length. The protein itself is very acidic and is very rich in aspartic acid ... The alanines are located adjacent to each other, amino acid number 233 and 234. Alanine 233 is highly conserved throughout the ... and glutamic acid. It is also very deficient in alanine, containing only two alanines in the entire sequence. ...
Cho WH, Lee YJ, Kong SI, Hurwitz J, Lee JK (2006). "CDC7 kinase phosphorylates serine residues adjacent to acidic amino acids ...
... the hydrolysis can be suppressed by adding an acid such as nitric acid, making the solution more acidic. Hydrolysis may proceed ... The hydrolysis of peptides gives amino acids. Many polyamide polymers such as nylon 6,6 hydrolyse in the presence of strong ... Strong acids also undergo hydrolysis. For example, dissolving sulfuric acid (H2SO4) in water is accompanied by hydrolysis to ... Trivalent ions like Al3+ and Fe3+ are weak acids whose pKa is comparable to that of acetic acid. Solutions of salts such as ...
"Salmonella enterica serovar typhimurium peptidase B is a leucyl aminopeptidase with specificity for acidic amino acids". J. ... Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp, but may be other amino ... acids, including Leu, Met, His, Cys and Gln. Mathew, Z.; Knox, T.M.; Miller, C.G. (2000). " ...
The full-length transcript of the mdm2 gene encodes a protein of 491 amino acids with a predicted molecular weight of 56kDa. ... The Mdm2 protein also contains a central acidic domain (residues 230-300). The phosphorylation of residues within this domain ... Mdm2 also contains a C-terminal RING domain (amino acid resdiues 430-480), which contains a Cis3-His2-Cis3 consensus that ... Additionally, phosphorylation at certain residues within the central acidic domain of Mdm2 may stimulate its ability to target ...
The amino acid sequence is 830 residues long and contains an acidic tail. 1 MVEEENIRVV RCGGSELNFR RAVFSADSKY IFCVSGDFVK ... Conservation of specific amino acids from positions 340-390, 430- 450, and 515-530 all correlate to predicted alpha helicies. " ...
1995). "Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic ... Liu J, Sessa WC (1994). "Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase ... Zhou W, Parent LJ, Wills JW, Resh MD (1994). "Identification of a membrane-binding domain within the amino-terminal region of ... 1985). "Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein". Science. 227 (4685): 427 ...
Glutamic Acid, Aspartic Acid, Amino Acid is $6.89. Free shipping on all orders over $35.00. ... Acidic Amino Acids : Glutamic Acid, Aspartic Acid, Amino Acid Neurotransmitter, Amino Acid Activation. by Not Available *ISBN13 ... 9781158327492 Our cheapest price for Acidic Amino Acids : ...
... polyoxyalkylene higher alcohol ethers and polyalkyleneglycol higher fatty acid monoesters. These diesters are useful as oil- ... N-long chain acyl-acidic glutamic or aspartic acid diesters having an acyl group of 8-22 carbon atoms, the ester part of which ... an acidic amino acid is reacted with an alcohol in the presence of an acidic catalyst to form a corresponding acidic amino acid ... or fatty acids (including branched fatty acids) obtainable by snythesis. The acidic amino acid component may be either an ...
Acidic amino acid antagonists and phencyclidine (PCP) agonists... ... Kynurenic acid inhibits synaptic and acidic amino acid-induced ... Acidic amino acid antagonists and phencyclidine (PCP) agonists were evaluated for their ability to protect neurons from the ... Hippocampal Neuron Hippocampal Slice Acidic Amino Acid Population Spike Stratum Pyramidale These keywords were added by machine ... Olney, J. W., Ho, O. C., and Rhee, V., 1971, Cytotoxic effects of acidic and sulphur containing amino acids on the infant mouse ...
Arachidonic Acid Mossy Fiber Acidic Amino Acid Cyclooxygenase Inhibitor Exogenous Fatty Acid These keywords were added by ... Levi, G., Gordon, R. D., Gallo, V., Wilkin, G. P. and Balazs, R., Putative acidic amino acid transmitters in the cerebellum I. ... Terrian D.M., Bischoff S.B., Schwartz M.A., Dorman R.V. (1987) Molecular Mechanisms of Acidic Amino Acid Release from Mossy ... Molecular Mechanisms of Acidic Amino Acid Release from Mossy Fiber Terminals of Rat Cerebellum. ...
... cysteine sulfinic acid, and cysteic acid to beta-alanine, hypotaurine and taurine, respectively. Does not exhibit any ... Acidic amino acid decarboxylase GADL1Add BLAST. 521. Amino acid modifications. Feature key. Position(s). DescriptionActions. ... sp,Q6ZQY3,GADL1_HUMAN Acidic amino acid decarboxylase GADL1 OS=Homo sapiens GN=GADL1 PE=1 SV=4 ... R-HSA-70614. Amino acid synthesis and interconversion (transamination). Miscellaneous databases. ChiTaRS: a database of human, ...
... is a single cluster of basic amino acids (PKKKRKV132; single-letter code, the basic amino acids are shown in bold; [4,5]), ... Comparative mutagenesis of nuclear localization signals reveals the importance of neutral and acidic amino acids.. Makkerh JP1 ... Contrary to conventional views, neutral and even acidic amino acids can play crucial roles in NLSs. ... The nucleoplasmin NLS requires two essential clusters of basic amino acids, separated by a mutation-tolerant spacer ( ...
Both Basic and Acidic Amino Acid Residues of Are Involved in Triggering Substate of RyR1. In Ra Seo,1,2 Dae Eun Kang,1,2 Dong ... In Ra Seo, Dae Eun Kang, Dong Woo Song, and Do Han Kim, "Both Basic and Acidic Amino Acid Residues of Are Involved in ...
Variation in the morphology of nanoparticles could be consistent with the difference in the affinity of amino acids binding at ... Hydroxyapatite synthesized with aspartic acid showed smooth flake-like morphology at pH= 11 and flake-like morphology with ... stripes at pH= 8. However, hydroxyapatite synthesized in the present of glutamic acid showed rod-like morphology at both pH ... Hydroxyapatite nanoparticles were synthesized in the presence of two kinds of acidic amino acids in order to investigate the ...
141 Amino Acid Form with Amino Terminal His Tag AND LEU 44 REPLACED BY PHE AND LEU 73 REPLACED BY VAL AND VAL 109 REPLACED BY ... Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 44 REPLACED BY PHE AND LEU 73 ... Human acidic fibroblast growth factor (FGF-1) is a member of the beta-trefoil hyperfamily and exhibits a characteristic ... Human acidic fibroblast growth factor (FGF-1) is a member of the beta-trefoil hyperfamily and exhibits a characteristic ...
Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 44 REPLACED BY PHE (L44F). ... Acids Res. 2008 36: D419-D425 * [4] Alexandrov N., Shindyalov I. (2003). PDP: protein domain parser.. Bioinformatics 2003 Feb; ... Description: acidic fibroblast growth factor protein , Length: 146 No structure alignment results are available for 1JTC.A, ...
The effects of excitatory amino acids on 22Na efflux rate in rat hippocampal slices were determined at various postnatal days ... Hepatocyte heterogeneity in the metabolism of amino acids and ammonia.. 12173653 - Enantioselective uptake of amino acids using ... Glutamic Acid. Hippocampus / growth & development, metabolism*. Rats. Rats, Inbred Strains. Receptors, Amino Acid. Receptors, ... Classification and properties of acidic amino acid receptors in hippocampus. III. Supersensitivity during the postnatal period ...
Epub ahead of print] A Single Amino Acid at the Polymerase Acidic Protein Determines the Pathogenicity of Influenza B Viruses. ... A Single Amino Acid at the Polymerase Acidic Protein Determines the Pathogenicity of Influenza B Viruses.. Bae JY1, Lee I1, Kim ... A Single Amino Acid at the Polymerase Acidic Protein Determines the Pathogenicity of Influenza B Viruses April 14th, 2018, 01: ... A Single Amino Acid at the Polymerase Acidic Protein Determines the Pathogenicity of Influenza B Viruses. ...
Acidic Flash Switching in a Micro-flow ReactorRapid and Mild Synthesis of Amino Acid N-Carboxy Anhydrides Using Basic-to-Acidic ... Rapid and Mild Synthesis of Amino Acid N-Carboxy Anhydrides Using Basic-to-Acidic Flash Switching in a Micro-flow Reactor. ... Rapid and Mild Synthesis of Amino Acid N-Carboxy Anhydrides Using Basic-to- ...
... and Acidic Amino Acids in Oat Coleoptiles" on DeepDyve, the largest online rental service for scholarly research with thousands ... and Acidic Amino Acids... Thomas B. Kinraide and Bud Etherton 1980-06-01 00:00:00 The application of neutral or acidic amino ... acidic, and basic amino acids. We suggest that the neutral amino acids are co-transported with a single H + and that ... acidic, and basic amino acids. We suggest that the neutral amino acids are co-transported with a single H + and that ...
... suggesting that an aromatic amino acid is not absolutely essential at position 65, but that glutamate 94 is essential for ... with a non-aromatic amino acid, or replacement of the glutamate at ferredoxin position 94, decreased the turnover number ... without detectable modification of other amino acids, and inhibits enzyme activity by 85% with either reduced ferredoxin or ... The role of aromatic and acidic amino acids in the electron transfer reaction catalyzed by spinach ferredoxin-dependent ...
The amino-acid pair predictability was used to transfer 2432 polymerase acidic proteins into 2432 scalar data. The one-way ... Thus, an important question is if these classifications are numerically distinguishable with respect to the polymerase acidic ... The polymerase acidic protein is an important family of proteins from influenza A virus, which is classified as many different ... ANOVA found these polymerase acidic proteins distinguish-able in terms of subtypes and species. However, the large residuals in ...
... proline and acidic amino acid-rich basic leucine zipper) transcription factor family. \ 27-516 for more molecular products just ... amino acid conjugation of benzoic acid. WP662: Amino Acid metabolism. WP7: Sulfur Amino Acid biosynthesis. WP715: amino acid ... WP1008: amino acid conjugation of benzoic acid. WP1127: amino acid conjugation of benzoic acid. WP1252: amino acid conjugation ... WP1287: amino acid conjugation of benzoic acid. WP1531: Vitamin D synthesis. WP1577: amino acid conjugation of benzoic acid. ...
... amino acid residues 1-85), B boxes (amino acid residues 88-162) and a C-terminal acidic tail (amino acid residues 186-215). ... The sequence of HMGB1 amino acid residues 201-205 is EDEED which are all acidic amino acid residues but no data and references ... is also called C-terminal acidic tail because it is full of acidic amino acid residues such as aspartate and glutamic acid [5-8 ... eleven different deleted mutants lacking several amino acid residues in C-terminal acidic tail of HMGB1 (rHMGB1 lacking amino ...
Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view. Length. ... section describes the position of regions of compositional bias within the protein and the particular amino acids that are over ... The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, ... Asp/Glu-rich (highly acidic)Add BLAST. 110. ,p>This subsection of the Family and domains section provides general information ...
We are Professional Manufacturer of Acidic Amino Acids company, Factory & Exporters specialize in Acidic Amino Acids wiht High- ... Find Acidic Amino Acids Manufacturers & Suppliers from China. ... Home > Products > Acidic Amino Acids. Acidic Amino Acids - ... We aim at becoming one of your most reliable partners and earning your satisfaction for Acidic Amino Acids , acidic amino acids ... Our organization has a top quality assurance procedure have already been established for Acidic Amino Acids , acidic amino ...
... Chang, ... Acidic cluster; Ribosomal protein; Nuclear retention signal; Yeast two-hybrid; Ribosome assembly Identifiers. URN: urn:nbn:se: ... RpL22 normally enters the nucleolus via a compulsory sequence of KKYLKK (I-domain, positions 88-93). An acidic residue cluster ...
... starting with the structure and nature of amino acids, the general difference between acid... ... Learn about what differentiates acidic and basic amino acids, ... Acidic Amino Acids. The two acidic amino acids are:. *Aspartate ... Acidic and Basic Amino Acids. Of our amino acids, which are acidic, which are base, and why does it matter? First well state ... Acidic amino acids are also by their nature hydrophilic amino acids (meaning they like water, as opposed to hydrophobic amino ...
Amino Acids tutorial video explaining the hydrophilic side chain characteristics for polar neutral, acidic and basic amino acid ... Amino Acids 3 Polar Acidic and Basic Side Chains. Amino Acids 3 Polar Acidic and Basic Side Chains. March 7, 2016 By Leah4sci ... Watch Previous Video: Hydrophobic Amino Acids. - , Watch Next Video: Stereochemistry of Amino Acids D and L from R and S ... Watch on YouTube: Polar/Acidic/Basic Amino Acids. Click cc on the bottom right for video transcript) ...
Baking soda neutralizes acids in various circumstances, including inside the human body and in the environment. Baking soda, ... Is calcium carbonate acidic or basic?. * Q: Is sugar an acid or base?. ... What are ketogenic and glucogenic amino acids?. * Q: What is the pH of milk?. ... A list of strong acids includes hydrochloric acid, nitric acid, sulfuric acid, hydrobromic acid, hydroiodic acid, chloric acid ...
The amide is rather easily hydrolyzed, converting asparagine to aspartic acid. This process is thought to be one o ... Asparagine is the amide of aspartic acid. The amide group does not carry a formal charge under any biologically relevant pH ... Asparagine of acidic amino acids R-group. Asparagine is the amide of aspartic acid. The amide group does not carry a formal ... Tryptophan FunctionTryptophan is one of the 22 standard amino acids and an essential amino acid in .. ...
  • Analysis of concentration-response curves suggests that the increased responsiveness to L-glutamate is due to an increase in the maximal effect rather than to changes in the half-maximal concentration for the amino acid. (biomedsearch.com)
  • Partial denervation does not detectably change efflux elicited by D,L-homocysteic acid nor does it modify the properties of [3H]glutamate binding to hippocampal membranes. (biomedsearch.com)
  • The role of aromatic and acidic amino acids in the electron transfer reaction catalyzed by spinach ferredoxin-dependent glutamate synthase. (semanticscholar.org)
  • In E. coli , the acid-resistance systems 2 (AR2) and 3 (AR3) expel intracellular protons through two coupled processes: intracellular decarboxylation of glutamate (Glu) and arginine (Arg) by AR2 and AR3, respectively, and the exchange of the reaction products, γ-aminobutyric acid (GABA) and agmatine (Agm), with extracellular Glu and Arg ( 2 ). (sciencemag.org)
  • We have recently identified another member of this family as responsible for classical amino acid transport System N. Unlike the virtually ubiquitous Systems A, ASC, and L, System N appears more tissue-specific and mediates the uptake specifically of glutamine, histidine, and asparagine ( 25 ). (pnas.org)
  • Sodium bicarbonate is actually produced naturally by the pancreas to assist with neutralizing acids from food, but various lifestyle decisions negatively impact the pancreas' ability to produce this helpful material. (reference.com)
  • Examples are: citric acid (lemon juice), acetic acid (vinegar), stomach acid, and battery acid. (aminoco.com)
  • Weak acids include formic acid, acetic acid, hydrofluoric acid, hydrogen sulfide and hydrocyanic acid. (reference.com)
  • within approximately 1 pH unit of the pKa - (example) - solution containing acetic acid (HA = CH3COOH) and acetate (A- = CH3COO-) with a pKa of 4.8 resists a change in pH from pH 3.8 to 5.8, with maximum buffering at pH = 4.8. (scribd.com)
  • Common aqueous acids include hydrochloric acid (a solution of hydrogen chloride which is found in gastric acid in the stomach and activates digestive enzymes ), acetic acid (vinegar is a dilute aqueous solution of this liquid), sulfuric acid (used in car batteries ), and citric acid (found in citrus fruits). (wikipedia.org)
  • However, hydrogen chloride, acetic acid, and most other Brønsted-Lowry acids cannot form a covalent bond with an electron pair and are therefore not Lewis acids. (wikipedia.org)
  • 3602 words - 14 pages was the most explosive, followed by the Citric and Acetic acid. (brightkite.com)
  • 2-{[(3,5-dihydroxyphenyl)(hydroxy)methylidene]amino}acetic acid belongs to the class of organic compounds known as hippuric acids. (hmdb.ca)
  • 2-{amino}acetic acid is a predicted metabolite generated by BioTransformer¹ that is produced by the metabolism of 3,5-dihydroxybenzoic acid. (hmdb.ca)
  • 2-{[(3,5-dihydroxyphenyl)(hydroxy)methylidene]amino}acetic acid is an extremely weak basic (essentially neutral) compound (based on its pKa). (hmdb.ca)
  • Salts of strong acids and strong bases ("strong salts") are non-volatile and odorless, whereas salts of either weak acids or weak bases ("weak salts") may smell like the conjugate acid (e.g., acetates like acetic acid (vinegar) and cyanides like hydrogen cyanide (almonds)) or the conjugate base (e.g., ammonium salts like ammonia) of the component ions. (wikipedia.org)
  • A list of acids and their sources includes hydrochloric acid, which is produced naturally in the stomach to help the body break down and digest food, and c. (reference.com)
  • 2014. Hydrochloric Acid (Hydrogen Chloride). (brightkite.com)
  • Amino acids are organic compounds made of carbon, hydrogen, oxygen, nitrogen, and (in some cases) sulfur bonded in characteristic formations. (encyclopedia.com)
  • Amino acids are organic compounds, meaning that they contain carbon and hydrogen bonded to each other. (encyclopedia.com)
  • Due to the two charges on zwitterions, there is a much stronger intermolecular attraction between the ions, raising the melting point of an amino acid far above the melting point of organic compounds with similar molecular mass and numbers of electrons . (conservapedia.com)
  • Acidic products from BioAyurveda a combination of organic herbs and herbal nutrient sources that is formulated to empower digestive functioning and gut health that are at the core of overall health and vitality. (selfgrowth.com)
  • TD Product Details: Minimum Order Quantity 100 Kilogram Form Powder Organic Type Organic Pack Size 25 kg Packaging Type Bag Physical State Powder Purity (%) 100% Usage AGRICULTURE We offer Amino Acid Powder which is a natural extract from ancient. (tradeindia.com)
  • Organic compound containing both basic amino and acidic carobxyl groups. (marxist.com)
  • Hydrogen molecules are why bases and acids are often measured in pH levels (pH stands for "potential of hydrogen") as related to pure water. (aminoco.com)
  • Interestingly, nearly all of the amino acids occurring in nature are the left-hand versions of the molecules, or the L-forms. (encyclopedia.com)
  • These twenty amino acids are biosynthesized from other molecules, but organisms differ in which ones they can synthesize and which ones must be provided in their diet. (wikidoc.org)
  • The charged state of an amino acid in aqueous solution depends largely on the pH. (wikibooks.org)
  • The PSP mouse bioassay involves acidic aqueous extraction of the tissue (whole animal or selected organs) followed by intraperitoneal injection of 1 ml of the extract into mice. (fao.org)
  • In the special case of aqueous solutions, proton donors form the hydronium ion H 3 O + and are known as Arrhenius acids . (wikipedia.org)
  • Aqueous Arrhenius acids have characteristic properties which provide a practical description of an acid. (wikipedia.org)
  • Acids form aqueous solutions with a sour taste, can turn blue litmus red, and react with bases and certain metals (like calcium ) to form salts . (wikipedia.org)
  • An aqueous solution of an acid has a pH less than 7 and is colloquially also referred to as 'acid' (as in 'dissolved in acid'), while the strict definition refers only to the solute . (wikipedia.org)
  • Most acids encountered in everyday life are aqueous solutions , or can be dissolved in water, so the Arrhenius and Brønsted-Lowry definitions are the most relevant. (wikipedia.org)
  • Iodinated and brominated tyrosine are also amino acids found in species, but are not included in the 20 major amino acids because of their rarity: iodinated tyrosin is only found in thyroid hormones, and brominated tyrosine is only found in coral. (wikibooks.org)
  • We suggest that the neutral amino acids are co-transported with a single H + and that accumulation depends upon both the ΔpH and the membrane potential components of the proton motive force. (deepdyve.com)