Peptide Chain Initiation, Translational: A process of GENETIC TRANSLATION whereby the formation of a peptide chain is started. It includes assembly of the RIBOSOME components, the MESSENGER RNA coding for the polypeptide to be made, INITIATOR TRNA, and PEPTIDE INITIATION FACTORS; and placement of the first amino acid in the peptide chain. The details and components of this process are unique for prokaryotic protein biosynthesis and eukaryotic protein biosynthesis.Peptide Initiation Factors: Protein factors uniquely required during the initiation phase of protein synthesis in GENETIC TRANSLATION.Ribosomes: Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.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.Peptide Chain Elongation, Translational: A process of GENETIC TRANSLATION, when an amino acid is transferred from its cognate TRANSFER RNA to the lengthening chain of PEPTIDES.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.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.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.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.Reticulocytes: Immature ERYTHROCYTES. In humans, these are ERYTHROID CELLS that have just undergone extrusion of their CELL NUCLEUS. They still contain some organelles that gradually decrease in number as the cells mature. RIBOSOMES are last to disappear. Certain staining techniques cause components of the ribosomes to precipitate into characteristic "reticulum" (not the same as the ENDOPLASMIC RETICULUM), hence the name reticulocytes.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.RNA, Transfer: The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.Peptide Biosynthesis: The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules.Puromycin: A cinnamamido ADENOSINE found in STREPTOMYCES alboniger. It inhibits protein synthesis by binding to RNA. It is an antineoplastic and antitrypanosomal agent and is used in research as an inhibitor of protein synthesis.Eukaryotic Initiation Factor-2: Eukaryotic initiation factor of protein synthesis. In higher eukaryotes the factor consists of three subunits: alpha, beta, and gamma. As initiation proceeds, eIF-2 forms a ternary complex with Met-tRNAi and GTP.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Kinetics: The rate dynamics in chemical or physical systems.Polyribosomes: A multiribosomal structure representing a linear array of RIBOSOMES held together by messenger RNA; (RNA, MESSENGER); They represent the active complexes in cellular protein synthesis and are able to incorporate amino acids into polypeptides both in vivo and in vitro. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Ribosomal Proteins: Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits.RNA, Transfer, Amino Acyl: Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.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.Guanosine Triphosphate: Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.Decapoda (Crustacea): The largest order of CRUSTACEA, comprising over 10,000 species. They are characterized by three pairs of thoracic appendages modified as maxillipeds, and five pairs of thoracic legs. The order includes the familiar shrimps, crayfish (ASTACOIDEA), true crabs (BRACHYURA), and lobsters (NEPHROPIDAE and PALINURIDAE), among others.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.Molecular Weight: The sum of the weight of all the atoms in a molecule.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.Peptide Chain Termination, Translational: A process of GENETIC TRANSLATION whereby the terminal amino acid is added to a lengthening polypeptide. This termination process is signaled from the MESSENGER RNA, by one of three termination codons (CODON, TERMINATOR) that immediately follows the last amino acid-specifying CODON.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.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.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.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).Bacterial Proteins: Proteins found in any species of bacterium.Guanine NucleotidesAmino 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.Poly U: A group of uridine ribonucleotides in which the phosphate residues of each uridine ribonucleotide act as bridges in forming diester linkages between the ribose moieties.RNA, Bacterial: Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis.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.Cell-Free System: A fractionated cell extract that maintains a biological function. A subcellular fraction isolated by ultracentrifugation or other separation techniques must first be isolated so that a process can be studied free from all of the complex side reactions that occur in a cell. The cell-free system is therefore widely used in cell biology. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p166)Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.RNA, Transfer, Met: A transfer RNA which is specific for carrying methionine to sites on the ribosomes. During initiation of protein synthesis, tRNA(f)Met in prokaryotic cells and tRNA(i)Met in eukaryotic cells binds to the start codon (CODON, INITIATOR).Oligopeptides: Peptides composed of between two and twelve amino acids.N-Formylmethionine: Effective in the initiation of protein synthesis. The initiating methionine residue enters the ribosome as N-formylmethionyl tRNA. This process occurs in Escherichia coli and other bacteria as well as in the mitochondria of eucaryotic cells.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.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.Ribosome Subunits, Small, Bacterial: The small subunit of eubacterial RIBOSOMES. It is composed of the 16S RIBOSOMAL RNA and about 23 different RIBOSOMAL PROTEINS.Guanosine Diphosphate: A guanine nucleotide containing two phosphate groups esterified to the sugar moiety.Ribosome Subunits: The two dissimilar sized ribonucleoprotein complexes that comprise a RIBOSOME - the large ribosomal subunit and the small ribosomal subunit. The eukaryotic 80S ribosome is composed of a 60S large subunit and a 40S small subunit. The bacterial 70S ribosome is composed of a 50S large subunit and a 30S small subunit.Peptide Termination Factors: Proteins that are involved in the peptide chain termination reaction (PEPTIDE CHAIN TERMINATION, TRANSLATIONAL) on RIBOSOMES. They include codon-specific class-I release factors, which recognize stop signals (TERMINATOR CODON) in the MESSENGER RNA; and codon-nonspecific class-II release factors.Aurintricarboxylic Acid: A dye which inhibits protein biosynthesis at the initial stages. The ammonium salt (aluminon) is a reagent for the colorimetric estimation of aluminum in water, foods, and tissues.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.Peptide Library: A collection of cloned peptides, or chemically synthesized peptides, frequently consisting of all possible combinations of amino acids making up an n-amino acid peptide.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.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.Artemia: A genus of CRUSTACEA of the order ANOSTRACA, found in briny pools and lakes and often cultured for fish food. It has 168 chromosomes and differs from most crustaceans in that its blood contains hemoglobin.RNA, Ribosomal: The most abundant form of RNA. Together with proteins, it forms the ribosomes, playing a structural role and also a role in ribosomal binding of mRNA and tRNAs. Individual chains are conventionally designated by their sedimentation coefficients. In eukaryotes, four large chains exist, synthesized in the nucleolus and constituting about 50% of the ribosome. (Dorland, 28th ed)Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.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).Peptide Elongation Factors: Protein factors uniquely required during the elongation phase of protein synthesis.Recombinant Proteins: Proteins prepared by recombinant DNA technology.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.Ribosome Subunits, Large, Eukaryotic: The large subunit of the 80s ribosome of eukaryotes. It is composed of the 28S RIBOSOMAL RNA, the 5.8S RIBOSOMAL RNA, the 5S RIBOSOMAL RNA, and about 50 different RIBOSOMAL PROTEINS.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.Ribosome Subunits, Large, Bacterial: The large subunit of the eubacterial 70s ribosome. It is composed of the 23S RIBOSOMAL RNA, the 5S RIBOSOMAL RNA, and about 37 different RIBOSOMAL PROTEINS.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.Pactamycin: Antibiotic produced by Streptomyces pactum used as an antineoplastic agent. It is also used as a tool in biochemistry because it inhibits certain steps in protein synthesis.Centrifugation, Density Gradient: Separation of particles according to density by employing a gradient of varying densities. At equilibrium each particle settles in the gradient at a point equal to its density. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.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.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.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Cell Line: Established cell cultures that have the potential to propagate indefinitely.TritiumAmino 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.DNA-Directed RNA Polymerases: Enzymes that catalyze DNA template-directed extension of the 3'-end of an RNA strand one nucleotide at a time. They can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to alpha-amanitin, and the type of RNA synthesized. (From Enzyme Nomenclature, 1992).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.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Antimicrobial Cationic Peptides: Small cationic peptides that are an important component, in most species, of early innate and induced defenses against invading microbes. In animals they are found on mucosal surfaces, within phagocytic granules, and on the surface of the body. They are also found in insects and plants. Among others, this group includes the DEFENSINS, protegrins, tachyplesins, and thionins. They displace DIVALENT CATIONS from phosphate groups of MEMBRANE LIPIDS leading to disruption of the membrane.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.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.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.Ribosome Inactivating Proteins, Type 1: Ribosome inactivating proteins consisting of only the toxic A subunit, which is a polypeptide of around 30 kDa.Ribosome Subunits, Small, Eukaryotic: The small subunit of the 80s ribosome of eukaryotes. It is composed of the 18S RIBOSOMAL RNA and 32 different RIBOSOMAL PROTEINS.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)Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Peptides, Cyclic: Peptides whose amino and carboxy ends are linked together with a peptide bond forming a circular chain. Some of them are ANTI-INFECTIVE AGENTS. Some of them are biosynthesized non-ribosomally (PEPTIDE BIOSYNTHESIS, NON-RIBOSOMAL).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.Carcinoma, Ehrlich Tumor: A transplantable, poorly differentiated malignant tumor which appeared originally as a spontaneous breast carcinoma in a mouse. It grows in both solid and ascitic forms.Nucleic Acid Conformation: The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.Amino Acid Transport Systems: Cellular proteins and protein complexes that transport amino acids across biological membranes.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.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: 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).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.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.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).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.RNA, Viral: Ribonucleic acid that makes up the genetic material of viruses.Genes, Bacterial: The functional hereditary units of BACTERIA.Peptide Elongation Factor Tu: A protein found in bacteria and eukaryotic mitochondria which delivers aminoacyl-tRNA's to the A site of the ribosome. The aminoacyl-tRNA is first bound to a complex of elongation factor Tu containing a molecule of bound GTP. The resulting complex is then bound to the 70S initiation complex. Simultaneously the GTP is hydrolyzed and a Tu-GDP complex is released from the 70S ribosome. The Tu-GTP complex is regenerated from the Tu-GDP complex by the Ts elongation factor and GTP.Polyketide Synthases: Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES and other polyketides.Codon, Terminator: Any codon that signals the termination of genetic translation (TRANSLATION, GENETIC). PEPTIDE TERMINATION FACTORS bind to the stop codon and trigger the hydrolysis of the aminoacyl bond connecting the completed polypeptide to the tRNA. Terminator codons do not specify amino acids.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.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.PolynucleotidesPhosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Uracil NucleotidesSpecies 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.Oviducts: Ducts that serve exclusively for the passage of eggs from the ovaries to the exterior of the body. In non-mammals, they are termed oviducts. In mammals, they are highly specialized and known as FALLOPIAN TUBES.Lysine: An essential amino acid. It is often added to animal feed.Peptide Synthases: Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.Protein PrecursorsPeptide Elongation Factor G: Peptide Elongation Factor G catalyzes the translocation of peptidyl-tRNA from the A to the P site of bacterial ribosomes by a process linked to hydrolysis of GTP to GDP.Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
During chain elongation, each additional amino acid is added to the nascent polypeptide chain in a three-step microcycle. The ... The ribosome can be trafficked to the start site by direct binding, initiation factors, and/or ITAFs (IRES trans-acting factors ... Ribosomal pausing also aids co-translational folding of the nascent polypeptide on the ribosome, and delays protein translation ... forming the peptide bond and (3) shifting the mRNA by one codon relative to the ribosome. Unlike bacteria, in which translation ...
... the ribosome attaches its amino acid cargo to the new polypeptide chain, which is synthesized from amino terminus to carboxyl ... Gene expression can be regulated at any step: from transcriptional initiation, to RNA processing, to post-translational ... for carrying out the chemical reactions to add new amino acids to a growing polypeptide chain by the formation of peptide bonds ... each correspond to a specific amino acid. The principle that three sequential bases of DNA code for each amino acid was ...
The ribosome creates the protein chain by following the mRNA code and integrating the amino acid of an aminoacyl-tRNA (also ... a peptide bond is formed between the growing polypeptide chain on the P-site tRNA and the amino acid of the A-site tRNA, and ... such that anticodon-codon binding in the ribosome alone is not sufficient to maintain high translational fidelity. This is ... EF-Tu • GTP binds all correctly-charged aa-tRNAs with approximately identical affinity, except those charged with initiation ...
... of the peptide chain of the protein to be encoded and the A site has the next amino acid to be added to the peptide chain. The ... which help the assembly of the initiation complex. Variations in the mechanism can be anticipated. The ribosome has three ... All translational components are now free for additional rounds of translation. Translation is carried out by more than one ... And the E site which is the exit site of the now uncharged tRNA after it gives its amino acid to the growing peptide chain. The ...
There is also one polypeptide chain that measures in at 26 amino acids. Conventionally, the rRNA is labeled with "H#" to ... "On the aminoacyl-tRNA binding site of the 30-S ribosomal subunit and its relation to the chain initiation site of the ribosome ... L Gold; D Pribnow; T Schneider; S Shinedling; B S Singer; Stormo, and G. (1981). "Translational Initiation in Prokaryotes". ... Proteins are labelled "S#" to indicate the different peptides involved in rRNA stablization. S11 and H45 are located near the ...
Methylation of Lysine (amino acid). Once the peptide chain is synthesized, it still must be modified. Post-translational ... After translational initiation (which is different in prokaryotes and eukaryotes), the ribosome enters the elongation period ... Amino Acid SynthesisEdit. Pathways that form each amino acid[4]. Amino Acid R-group‡ Pathway* ... These amino acids are known as non-essential amino acids. Essential amino acids require intermediates not present in the human ...
When the tRNA has an amino acid linked to it, it is termed "charged". Initiation involves the small subunit of the ribosome ... C-terminal or internal amino-acid residues or peptides from the polypeptide. The termini and side-chains of the polypeptide may ... co-translational transport, and post-translational modification. Protein biosynthesis is strictly regulated at multiple steps. ... The amino acids are then linked together to extend the growing protein chain, and the tRNAs, no longer carrying amino acids, ...
They include the 22 proteinogenic ("protein-building") amino acids, which combine into peptide chains ("polypeptides") to form ... "The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor ... While L-amino acids represent all of the amino acids found in proteins during translation in the ribosome, D-amino acids are ... The phrase "branched-chain amino acids" or BCAA refers to the amino acids having aliphatic side chains that are non-linear; ...
After the new amino acid is added to the chain, and after the mRNA is released out of the nucleus and into the ribosome's core ... Then, a peptide bond forms between the amino acid of the tRNA in the A site and the amino acid of the charged tRNA in the P ... When the tRNA has an amino acid linked to it, the tRNA is termed "charged". Initiation involves the small subunit of the ... In co-translational translocation, the entire ribosome/mRNA complex binds to the outer membrane of the rough endoplasmic ...
... and the basic 25-amino-acid peptide RPL41 is positioned at the subunit interface in the 80S ribosome, interacting with rRNA ... "Molecular architecture of a eukaryotic translational initiation complex". Science. 342 (6160): 1240585. doi:10.1126/science. ... and covalently links the amino acids into a polypeptide chain. Ribosomes from all organisms share a highly conserved catalytic ... "80S Ribosomes, Eukaryotic Ribosomes, Prokaryotic Ribosomes, Nucleic Acids, Sedimentation Coefficient". www. ...
Ribosomes can bind to a messenger RNA chain and use its sequence for determining the correct sequence of amino acids. Amino ... Specialized ribosomes[edit]. Heterogeneity in ribosome composition has been proposed to be involved in translational control of ... Rodnina, M.V.; Beringer, M.; Wintermeyer, W. (January 2007). "How ribosomes make peptide bonds". Trends Biochem. Sci. 32 (1): ... as well as much about the 40S subunit's interaction with eIF1 during translation initiation.[21] Similarly, the eukaryotic 60S ...
Amino acids are then chained together by the ribosome according to the order of triplets in the coding region. The ribosome ... particle-a protein that binds to the ribosome and directs it to the endoplasmic reticulum when it finds a signal peptide on the ... Poly(A) tail is bound by multiple poly(A)-binding proteins (PABP) necessary for mRNA export and translation re-initiation. A ... Any step of gene expression may be modulated, from the DNA-RNA transcription step to post-translational modification of a ...
"The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor ... Rodnina MV, Beringer M, Wintermeyer W (Januari 2007). "How ribosomes make peptide bonds". Trends in Biochemical Sciences 32 (1 ... van Heijenoort J (Machi 2001). "Formation of the glycan chains in the synthesis of bacterial peptidoglycan". Glycobiology 11 (3 ... Hylin, John W. (1969). "Toxic peptides and amino acids in foods and feeds". Journal of Agricultural and Food Chemistry 17 (3): ...
These are formed by post-translational modification of the side chains of standard amino acids present in the target protein. ... "The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor ... β-alanine: an amino acid produced by aspartate 1-decarboxylase and a precursor to coenzyme A and the peptides carnosine and ... "Evidence for the existence in mRNAs of a hairpin element responsible for ribosome dependent pyrrolysine insertion into proteins ...
... amino acids - amino terminus - amp resistance - amplification - amplicon - anchor sequence - animal model - anneal - anti-sense ... post-translational modification - post-translational processing - post-translational regulation - PRE - Precursor mRNA - ... ribonucleic acid - riboprobe - ribosomal binding sequence - ribosome - ribozyme - risk communication - RNA polymerase - RNA ... peptide - peptide bond - phage - phagemid - phenotype - phosphatase, alkaline - phosphodiester bond - phosphorylation - ...
"The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor ... Rodnina MV, Beringer M, Wintermeyer W (January 2007). "How ribosomes make peptide bonds". Trends in Biochemical Sciences 32 (1 ... It lacks the NH2 group because of the cyclization of the side-chain and is known as an imino acid; it falls under the category ... Hylin, John W. (1969). "Toxic peptides and amino acids in foods and feeds". Journal of Agricultural and Food Chemistry 17 (3): ...
Translation is accomplished by the ribosome, which links amino acids in an order specified by messenger RNA (mRNA), using ... Translation starts with a chain-initiation codon or start codon. The start codon alone is not sufficient to begin the process. ... This feature could allow accurate decoding absent complex translational machinery such as the ribosome, such as before cells ... Once enough peptides were coded for, any major random change in the genetic code would have been lethal; hence it became " ...
... another tRNA already bound to the ribosome transfers the growing polypeptide chain from its 3' end to the amino acid attached ... the aminoacyl-tRNA is bound in the A/A site and is ready for the next peptide bond to be formed to its attached amino acid. The ... In addition, the ribosome has two other sites for tRNA binding that are used during mRNA decoding or during the initiation of ... tRNA does this by carrying an amino acid to the protein synthetic machinery of a cell (ribosome) as directed by a 3-nucleotide ...
... s carry out a number of other functions, including fatty acid synthesis, much amino acid synthesis, and the immune ... Hirose, T; Sugiura, M (January 2004). "Functional Shine-Dalgarno-like sequences for translational initiation of chloroplast ... The ribosomes in chloroplasts are similar to bacterial ribosomes. Because so many chloroplast genes have been moved to the ... Chloroplast polypeptide chains probably often travel through the two complexes at the same time, but the TIC complex can also ...
... embedded in the lipid bilayer that allow protons to travel through the membrane by transferring from one amino acid side chain ... The rough ER has ribosomes attached to it used for protein synthesis, while the smooth ER is used more for the processing of ... "Post-Translational Modifications and Quality Control in the Rough ER". Molecular Cell Biology (4th ed.). ... "The role of the axolemma in the initiation of traumatically induced axonal injury" (PDF). Journal of Neurology, Neuroscience ...
... can then form a covalent link to the growing peptide chain allowing the mRNA to be physically linked to its translational ... that causes premature chain termination during translation taking place in the ribosome. Part of the molecule resembles the 3' ... 3'-deoxy-N,N-dimethyl-3'-[(O-methyl-L-tyrosyl)amino]adenosine ... initiation inhibitors). -mycin (Streptomyces). *Streptomycin#. ... It enters the A site and transfers to the growing chain, causing the formation of a puromycylated nascent chain and premature ...
Ribosome-nascent chain complex (RNC). *Post-translational modification (functional groups · peptides · structural changes) ... "Nucleic Acids Research. 10 (8): 2709-21. doi:10.1093/nar/10.8.2709. PMC 320645. PMID 7079182.. ... Loss of amino-groups occurs with a high frequency for cytosines, with different consequences depending on their methylation. ... "Nucleic Acids Research. 35 (6): e41. doi:10.1093/nar/gkm013. PMC 1874596. PMID 17289753.. ...
The amino acids in a polypeptide chain are linked by peptide bonds. Once linked in the protein chain, an individual amino acid ... Ribosome-nascent chain complex (RNC). *Post-translational modification (functional groups · peptides · structural changes) ... راه‌اندازی در نزدیکی جایگاه آغاز رونویسی (initiation site) قرار دارد. جایگاه آغاز رونویسی، به اولین نوکلئوتیدی از DNA گفته ... The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino ...
Amino acid synthesis. Chloroplasts alone make almost all of a plant cell's amino acids in their stroma[158] except the sulfur- ... Hirose, T; Sugiura, M (January 2004). "Functional Shine-Dalgarno-like sequences for translational initiation of chloroplast ... Chloroplast ribosomes Comparison of a chloroplast ribosome (green) and a bacterial ribosome (yellow). Important features common ... which holds the acyl chain as it is synthesized. The initiation of synthesis begins with the condensation of malonyl-ACP with ...
Once the tRNA is charged, a ribosome can transfer the amino acid from the tRNA onto a growing peptide, according to the genetic ... by directing an unnatural amino acid with a reactive side-chain into the binding site, create a new protein that cuts the DNA ... "Phosphorylation of glutamyl-prolyl tRNA synthetase by cyclin-dependent kinase 5 dictates transcript-selective translational ... beyond the twenty canonical amino acids found in nature, to include an unnatural amino acid as well. The unnatural amino acid ...
... embedded in the lipid bilayer that allow protons to travel through the membrane by transferring from one amino acid side chain ... The rough ER has ribosomes attached to it used for protein synthesis, while the smooth ER is used more for the processing of ... "Post-Translational Modifications and Quality Control in the Rough ER". Molecular Cell Biology (4th ed.). ... "The role of the axolemma in the initiation of traumatically induced axonal injury" (PDF). Journal of Neurology, Neuroscience ...
The binding is facilitated by ribosomes. The amino acids carried by tRNA from the polypeptide chain by peptide bond formation ... between two amino acids. This amino acid chain undergoes post-translational modifications and then folds into 3-D structure in ... Translation: Ribosomes are enzymes.. Initiation. Transcription: Binding of RNA polymerase into the promoter of the gene ... During translation, mRNA is decoded by ribosomes in order to produce an amino acid chain or a polypeptide chain. Complementary ...
As these steps are continued, the mRNA slides along the ribosome, three bases at a time, and the peptide (amino acid) chain ... In addition, some codons do not code for amino acids, but code for polypeptide chain initiation and termination. The genetic ... After being released from the tRNA, some proteins may undergo post-translational modifications. They may be cleaved by a ... for joining the amino acids. The amino acids are carried to the ribosome by the tRNAs. Each tRNA has a specific amino acid ...
During chain elongation, each additional amino acid is added to the nascent polypeptide chain in a three-step microcycle. The ... The ribosome can be trafficked to the start site by direct binding, initiation factors, and/or ITAFs (IRES trans-acting factors ... Ribosomal pausing also aids co-translational folding of the nascent polypeptide on the ribosome, and delays protein translation ... forming the peptide bond and (3) shifting the mRNA by one codon relative to the ribosome. Unlike bacteria, in which translation ...
Peptide chain elongation 67 Ribosome 38 Selenoamino acid metabolism 67 Selenocysteine synthesis 67 ... L13a-mediated translational silencing of Ceruloplasmin expression 67 Metabolism of amino acids and derivatives 67 ... Cap-dependent Translation Initiation 67 CFTR translational fidelity (class I mutations) 23 ... cellular amino acid biosynthetic process. GO:0008652 8.96. OAT PYCR1 3. L-proline biosynthetic process. GO:0055129 8.62. OAT ...
... the ribosome attaches its amino acid cargo to the new polypeptide chain, which is synthesized from amino terminus to carboxyl ... Gene expression can be regulated at any step: from transcriptional initiation, to RNA processing, to post-translational ... for carrying out the chemical reactions to add new amino acids to a growing polypeptide chain by the formation of peptide bonds ... each correspond to a specific amino acid. The principle that three sequential bases of DNA code for each amino acid was ...
Peptide chain elongation 65 Ribosome 36 Selenoamino acid metabolism 65 Selenocysteine synthesis 65 ... L13a-mediated translational silencing of Ceruloplasmin expression 65 Metabolism of amino acids and derivatives 65 ... Cap-dependent Translation Initiation 65 CFTR translational fidelity (class I mutations) 22 ... cellular amino acid biosynthetic process. GO:0008652 9.63. PYCR3 PYCR1 ALDH18A1 2. ethanol oxidation. GO:0006069 9.51. ALDH2 ...
... peptide hypothesis-the signal for a ribosome to attach to the rough ER resides in the first fifteen to thirty amino acids ... Initiation: The initiation amino acid in eukaryotes is methionine. Regulation of protein translation may occur in certain ... amino acid into a growing polypeptide chain because they retain the ability to read the codon corresponding to the amino acid ... Role of the amino acid in recognizing the anticodon for that amino acid: None. If an amino acid attached to the tRNA is ...
The experiments in vitro with the purified translation system show that ribosome recycling from initiation via protein ... the ribosome into its subunits after termination and that this step is the overture to ribosome recycling back to initiation of ... The fate of the mRNA after termination and ribosome recycling is highly relevant for translation of multicistronic mRNAs. The ... it is incompatible with the presence of RF1 on the ribosome. ... the inhibitory action of RF1 on ribosome recycling can be ...
... thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome ... and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Plays an important role in translational ... Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ... which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide ...
... is the term used to describe the process of protein synthesis by ribosomes in the cytoplasm or endoplasmic ... which are linked together by the ribosome. In this process, the mRNA is decoded to produce a specific amino acid chain, known ... base pairing occurs and the two amino acids are linked by the ribosome through a peptide bond. ... Following initiation, a new tRNA-amino acid complex enters the codon next to the AUG codon. If the anticodon of the new tRNA ...
... which normally targets nascent secretory peptides to the ER. BTF3 is also a general transcription factor that can form a stable ... Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition ... The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, ... NAC associates with ribosomes through the BTF3/NACB subunit. Both subunits can contact nascent polypeptide chains.1 Publication ...
The elements involved in both ribosome biogenesis and its function are extremely conserved in all organisms from the simplest ... In this process, named translation, the ribosome plays a central role. ... 2008) From one amino acid to another: tRNA-dependent amino acid biosynthesis. Nucleic Acids Res 36: 1813-1825. * View Article ... the peptide chain release factor RF1, the recycling factor RRF, the back translocation elongation factor LepA (also designated ...
d) the amino acids become joined by PEPTIDE BONDS, forming a polypeptide chain. Termination occurs when the ribosome encounters ... dispenses amino acids to a growing polypeptide chain; protein synthesis is divided into initiation, elongation and termination ... movement from one position to another along a straight or curved line (rectilinear or curvilinear motion). translational adj . ... along the mRNA beginning with the start codon specifies one amino acid in the polypeptide chain. See also deoxyribonucleic acid ...
After the peptide bond is formed, the peptide chain becomes bonded with tRNA2, which is located in the amino-acid area. ... Then a new aa-tRNA is bonded to the amino-acid area of the ribosome, and so on. During translation the ribosome moves along the ... The theory of translational symmetry plays an important role in crystallography and solid-state physics. For example, the ... differs in mechanism from the initiation and termination of translation, the signals for which are the bondings of ...
... amino acids of the stalled nascent peptide and the amino acid residue specified by the codon following the peak of the ribosome ... the first amino acid residue (presumably occupying the penultimate position of the nascent chain) and the incoming amino acids ... 1989) ermC leader peptide. Amino acid sequence critical for induction by translational attenuation. J Mol Biol 206(1):69-79. ... 1988) Extension inhibition analysis of translation initiation complexes. Methods Enzymol 164:419-425. ...
... amino acid of the] peptide might be the cognate amino acid, threonine (Mr = 119), with a mass shift of −30 Da relative to ... translational initiation and is, therefore, arranged like a messenger RNA (mRNA) with proper ribosome-binding site (RBS), AUG ... But how can ribosomes distinguish between AUG codons that signal addition of methionine (M, or Met) to a nascent peptide chain ... and the respective amino acid cova-lent-ly linked to the other end. Yet to make sense of the nume-rous amino acid-loaded tRNA ...
... amino acid analogs or derivatives, or substances recognized by the protein synthesizing machinery. Markers may comprise ... tRNA molecules are misaminoacylated with non-radioactive markers which may be non-native amino acids, ... Elongation proceeds with charged tRNAs binding to ribosomes, translocation and release of the amino acid cargo into the peptide ... amino acids that are derivatives of normal amino acids can be incorporated and only a few amino acid residues have side chains ...
Yarmolinsky, M. B., Haba, G. L. Inhibition by puromycin of amino acid incorporation into protein. Proc. Natl. Acad. Sci. U. S. ... Nathans, D. Puromuycin inhibition of protein synthesis: incorporation of puromycin into peptide chains. Proc. Natl. Acad. Sci. ... Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA… ... Algire, M. A. Development and characterization of a reconstituted yeast translation initiation system. RNA. 8, 382-397 (2002). ...
... vitro translational reactions in the presence of radioactively labeled amino acids to allow the detection of the nascent chains ... will as a rule slow down ribosome movement on the message and cause accumulation of nascent peptides of the respective sizes5-8 ... stage of transcript initiation, and (ii) an additional contribution to the specific recruitment of RNA polymerase into the ... Amino Acids, Peptides, and Proteins, De novo protein and peptide design, Drug design, In silico sequence selection, ...
The ribosome then carries out its priestly functions, uniting the new amino acid with the growing peptide chain through a ... more on translational initiation: http://bit.ly/2KNe00D. Amino acids are taken to the chapel by transfer RNAs (tRNAs) which ... In AMINO ACID ACTIVATION, an AMP molecule is added onto the amino acid from ATP. Then, in the tRNA CHARGING step, the amino ... youve gotta put down a deposit -, amino acid ACTIVATION (add AMP to amino acid) +$ ...
Methylation of Lysine (amino acid). Once the peptide chain is synthesized, it still must be modified. Post-translational ... After translational initiation (which is different in prokaryotes and eukaryotes), the ribosome enters the elongation period ... Amino Acid SynthesisEdit. Pathways that form each amino acid[4]. Amino Acid R-group‡ Pathway* ... These amino acids are known as non-essential amino acids. Essential amino acids require intermediates not present in the human ...
This chapter summarizes available information about translational gene organization and expression in Bacillus subtilis and ... the product of which removes the formyl group from the amino terminus of newly synthesized proteins. ... Tu to bring aminoacylated tRNA into the A site of the elongating ribosome, EF-Ts to recycle EF-Tu from its inactive GDP-bound ... state to the GTP-bound state required for tRNA binding, and EFG, which is required for translocation of the ribosome along the ...
It forms peptide bond between carboxy terminal of polypeptide chain and amino group of new amino acid. Polypeptide grows from ... Some initiation factor acts as helicases to relax secondary structure allowing small subunit to scan along the mRNA to find the ... Elongation: Ribosome moves forward placing empty tRNA in ___-site and tRNA with growing polypeptide in ___-site, leaving ___- ... P-site receives amino acid from A-site and adds it to the end of the amino acid side chain. ...
6. The polypeptide chain elongates one amino acid at a time, and peels away from the ribosome, folding up into a protein as it ... 4. The bond between the amino acid and the tRNA is cut and a peptide bond is formed between the two amino acids.. ... 1. A ribosome attaches to the mRNA at an initiation codon (AUG). The ribosome encloses two codons.. ... Post-Translational Modification [back to top]. In eukaryotes, proteins often need to be altered before they become fully ...
... the presence of massive post-translational modification of this plastid protein sub-fraction. The study provides an extended ... the presence of massive post-translational modification of this plastid protein sub-fraction. The study provides an extended ... Subsequent mass spectrometry of peptides isolated out of cut spots that had been treated with trypsin identified 58 different ... Subsequent mass spectrometry of peptides isolated out of cut spots that had been treated with trypsin identified 58 different ...
  • 1997). (A) The amount of peptidyl-tRNA remaining bound to ribosomes after 2 min of incubation with RF1, with and without 0.9 μM RF3 and with or without 0.2 mM GTP, is shown as a function of the amount of RF1 present. (asmscience.org)
  • B) The amount of peptidyl-tRNA remaining bound to ribosomes after incubation with 0.25 pmol of RF1 is shown as in panel A as a function of time of incubation. (asmscience.org)
  • Ribosomes are ribozymes , because the catalytic peptidyl transferase activity that links amino acids together is performed by the ribosomal RNA. (wikipedia.org)
  • The assembled ribosome has two tRNA-binding sites, which are called A- and P-site, for aminoacyl and peptidyl sites respectively. (powershow.com)
  • Finally, increased puromycin sensitivity was observed after depletion of eRF1 from the stalled ribosome complex, consistent with inhibition of peptidyl-tRNA hydrolysis resulting from an eRF1-uORF2 peptidyl-tRNA interaction. (asm.org)
  • The GGQ minidomain, located in an exposed area at the extreme tip of the middle domain, is invariant in all known class I release factors and is hypothesized to enable hydrolysis of the peptidyl-tRNA bond by the peptidyl transferase center of the ribosome ( 19 , 42 ). (asm.org)
  • Any peptide or protein that can be expressed as a sequence using the symbols in WIPO Standard ST.25 (1998), Appendix 2, Table 3 in conjunction with a description in the Feature section to describe, for example, modified linkages, cross links and end caps, non-peptidyl bonds, etc., is embraced by this definition. (uspto.gov)
  • Ribosomes are often associated with the intracellular membranes that make up the rough endoplasmic reticulum . (wikipedia.org)
  • eIF4A is an ATP-dependent RNA helicase, which aids the ribosome in resolving certain secondary structures formed along the mRNA transcript. (wikipedia.org)
  • Although footprinting experiments have implicated adenine at position 752 (domain II) in the binding of erythromycin, no direct interaction has been shown between the two structures, at least in the ribosome of D . radiodurans ( 17 , 35 ). (asm.org)
  • In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction. (proteopedia.org)
  • Backbone macrocyclic structures are often found in diverse bioactive peptides and contribute to greater conformational rigidity, peptidase resistance, and potential membrane permeability compared to their linear counterparts. (frontiersin.org)
  • We will compare biochemistry and the three-dimensional structures of ribosomes from modern organisms on particular lineages of the tree of life. (nasa.gov)
  • It is the 2-deoxystreptamine and the primed amino sugar (on the right in the structures shown in Fig. 1 ) which are essential for causing the lack of fidelity in the translation process ( 23 ). (asm.org)
  • 157) DEPARTMENT OF COMMERCE Patent and Trademark Office 37 CFR Part 1 [Docket No: 960828235-8109-RIN: 0651-AA88 Requirements for Patent Applications Containing Nucleotide Sequence and/or Amino Acid Disclosures AGENCY: Patent and Trademark Office, Commerce. (uspto.gov)
  • 7. The isolated nucleic acid of claim 5 , which comprises the nucleotide sequence of SEQ ID NO: 1. (google.com)
  • 22. An isolated oligonucleotide primer or probe of 50-100 nucleotides, wherein said oligonucleotide comprises at least 20 consecutive nucleotides of SEQ ID NO: 1 and hybridizes under highly stringent conditions of 0.2 SSC at 68 C. and a washing condition of 50% formamide, 4 SSC at 42 C. with a nucleic acid having the nucleotide sequence of SEQ ID NO: 1. (google.com)
  • For each coding triplet in the messenger RNA there is a distinct transfer RNA that matches and which carries the correct amino acid for that coding triplet. (wikipedia.org)