scholarly journals Multiple forms of histone H2B from the nematode Caenorhabditis elegans

1986 ◽  
Vol 235 (3) ◽  
pp. 769-773 ◽  
Author(s):  
J R Vanfleteren ◽  
S M Van Bun ◽  
L L Delcambe ◽  
J J Van Beeumen
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Amino Acid Sequence ◽  
Length Polymorphism ◽  
Polypeptide Chain ◽  
Multiple Forms ◽  
Nematode Caenorhabditis Elegans ◽  
Histone H2b ◽  
High Degree

The complete amino acid sequence of histone H2B from the nematode Caenorhabditis elegans was determined. The protein as obtained by us is a mixture of multiple forms. Approx. 90% of the molecules consist of a polypeptide chain of 122 amino acids with alanine as N-terminal residue and proline at the second position. In the remaining 10% alanine is lacking and the chain starts with proline. In addition to the heterogeneity of chain length, polymorphism occurs at the positions 7 (Ala/Lys), 14 (Ala/Lys) and 72 (Ala/Ser) of the major chain and at position 6 (Ala/Lys) of the shorter chain. In the N-terminal third of the molecule there is a high degree of sequence homology to the corresponding region in H2B from Drosophila (insect), Patella (mollusc) and Asterias (starfish). In contrast, this part of the molecule differs considerably from mammalian histone H2B.

scholarly journals Biophysics : Aspects of Amino Acids Sequence in Proteins and Nucleotide Sequence in Nucleic Acids

2013 ◽  
Vol 4 ◽  
pp. 65-74
Author(s):  
Khadka Bahadur Chhetri
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Nucleic Acids ◽  
Polypeptide Chain ◽  
Antibody Complex ◽  
Antigen Antibody

Protein is the polypeptide chain of amino-acid sequence. Proteins of all species, from bacteria to humans, are made up from the same set of 20 standard amino acids. In order to carry out their function they must take a particular shape which is known as fold. All the enzymes hormones and antibodies are also proteins. To treat certain toxic-microorganism or invader we need certain antigen-antibody complex in the organisms. Just as amino-acid sequence forms the proteins, the polynucleotide sequence forms the nucleic acids. The gene is a part of DNA macromolecule responsible for the synthesis of protein chains. There are 20 amino-acids responsible for the formation of protein and 4 nucleotides responsible for the formation of DNA (RNA). Therefore, we can say that protein text is written in 20-letter and the DNA (RNA) text is written in 4-letter language. The information contained in genes in DNA is transferred to mRNA during transcription.The Himalayan Physics Vol. 4, No. 4, 2013 Page: 65-74 Uploaded date: 12/23/2013 

The Croonian Lecture, 1966 - The genetic code

1967 ◽  
Vol 167 (1009) ◽  
pp. 331-347 ◽  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleic Acid ◽  
Amino Acid Sequence ◽  
Genetic Code ◽  
Polypeptide Chain ◽  
Amino Acid Residues ◽  
Standard Set ◽  
Polypeptide Chains

Genes are made of nucleic acid. Enzymes are made of protein. The amino acid sequence of a particular protein is synthesized under instruction from a particular piece of nucleic acid. Each protein is made of one or more polypeptide chains, synthesized by condensing together amino acids, head to tail, with the elimination of water. A typical polypeptide chain is several hundred amino acid residues long. Nevertheless only twenty different kinds of amino acids are commonly found in proteins. This standard set of twenty is the same throughout nature. Nucleic acid is made of polynucleotide chains. The repeating unit of the chain is a sugar (ribose for RNA , deoxyribose for DNA ) connected to a phosphate. A base is joined on to each sugar. There are four common bases in nucleic acid. DNA usually has adenine, guanine, cytosine and thymine. In RNA thymine is replaced by uracil.

Requirements for branched chain amino acids and their interactions in the nematode Caenorhabditis elegans

Nematology ◽  
2000 ◽  
Vol 2 (5) ◽  
pp. 501-506 ◽  
Author(s):  
Dalia Perelman ◽  
Nancy Lu
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Branched Chain Amino Acids ◽  
Nematode Caenorhabditis Elegans ◽  
Optimal Range ◽  
C Elegans ◽  
Branched Chain Amino Acid ◽  
High Concentrations ◽  
Branched Chain

AbstractBranched chain amino acid (BCAA) requirements and their interactions were studied in the nematode Caenorhabditis elegans. Optimal, deficiency and toxic levels affecting nematode population growth were determined for each of the three BCAAs. The optimal range for leucine was 0.72-2.8; for isoleucine, 0.86-1.7; and for valine, 0.51-4.1 mg ml-1. Leucine at high concentrations was toxic. When isoleucine and valine were both added at high concentrations, they also exerted a marked toxic effect. The interactions of the branched chain amino acids found among vertebrate animals were not observed in C. elegans. Les besoins relatifs aux amino-acides en chaîne ramifiée et leurs interactions chez le nématode Caenorhabditis elegans - Les besoins relatifs aux amino-acides en chaîne ramifiée (BCAA) et leurs interactions ont été étudiés chez le nématode Caenorhabditis elegans. Les niveaux optimal, de déficience et toxique affectant la croissance de la population du nématode ont été déterminés pour chacune des BCAA. L'optimum est, pour la leucine de 0,72 à 2,8, pour l'isoleucine de 0,86 à 1,7 et pour la valine de 0,51 à 4,1 mg ml-1. A forte concentration la leucine est toxique. Si l'isoleucine et la valine sont ajoutées à forte concentration elles exercent également une action toxique prononcée. Les interactions entre BCAA observées chez les vertébrés ne l'ont pas été chez les C. elegans.

scholarly journals Chymotryptic inhibitor I from potatoes. The amino acid sequence of subunit A*

1974 ◽  
Vol 137 (1) ◽  
pp. 101-112 ◽  
Author(s):  
M. Richardson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Polypeptide Chain ◽  
Proteinase Inhibitors ◽  
Dilute Acid ◽  
Subunit A ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of subunit A of the potato chymotryptic inhibitor I was determined. The sequence was deduced from analysis of fragments and peptides derived from the protein by cleavage with cyanogen bromide, N-bromosuccinimide and dilute acid, and by digestion with trypsin, thermolysin, pepsin and papain. The molecule consists of a single polypeptide chain of 84 residues, which contains two homologous regions each of 13 amino acids. The protein does not appear to be homologous with any other known proteinase inhibitors.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

Polypeptides Folding: Rules for the Calculation of the Backbone Dihedral Angles φ starting from the Amino Acid Sequence

2020 ◽  
Author(s):  
Michele Larocca
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Theoretical Approach ◽  
Polypeptide Chain ◽  
Hydrophobic Effect ◽  
Side Chain ◽  
Dihedral Angles ◽  
Mechanical Forces ◽  
Specific Chemical

<p>Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino acid sequence has not yet been revealed. The present study deals with these problematics and aims to furnish a possible explanation of the information contained in the amino acid sequence, showing and reporting rules to calculate the backbone dihedral angles φ. The study is based on the development of mechanical forces once specific chemical interactions are established among the side chain of the residues in a polypeptide chain. It aims to furnish a theoretical approach to predict backbone dihedral angles which, in the future, may be applied to computational developments focused on the prediction of polypeptide structures.</p>

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

Amino acid sequence of cyanogen bromide fragment CB5 of human hemopexin

1989 ◽  
Vol 54 (3) ◽  
pp. 803-810 ◽  
Author(s):  
Ivan Kluh ◽  
Ladislav Morávek ◽  
Manfred Pavlík
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acid Hydrolysis ◽  
Cyanogen Bromide ◽  
Polypeptide Chain ◽  
Amino Acid Residues ◽  
Mild Acid Hydrolysis ◽  
Methionine Residue ◽  
Cyanogen Bromide Fragment ◽  
Mild Acid

Cyanogen bromide fragment CB5 represents the region of the polypeptide chain of hemopexin between the fourth and fifth methionine residue (residues 232-352). It contains 120 amino acid residues in the following sequence: Arg-Cys-Ser-Pro-His-Leu-Val-Leu-Ser-Ala-Leu-Thr-Ser-Asp-Asn-His-Gly-Ala-Thr-Tyr-Ala-Phe-Ser-Gly-Thr-His-Tyr-Trp-Arg-Leu-Asp-Thr-Ser-Arg-Asp-Gly-Trp-His-Ser-Trp-Pro-Ile-Ala-His-Gln-Trp-Pro-Gln-Gly-Pro-Ser-Ala-Val-Asp-Ala-Ala-Phe-Ser-Trp-Glu-Glu-Lys-Leu-Tyr-Leu-Val-Gln-Gly-Thr-Gln-Val-Tyr-Val-Phe-Leu-Thr-Lys-Gly-Gly-Tyr-Thr-Leu-Val-Ser-Gly-Tyr-Pro-Lys-Arg-Leu-Glu-Lys-Glu-Val-Gly-Thr-Pro-His-Gly-Ile-Ile-Leu-Asp-Ser-Val-Asp-Ala-Ala-Phe-Ile-Cys-Pro-Gly-Ser-Ser-Arg-Leu-His-Ile-Met. The sequence was derived from the data on peptides prepared by cleavage of fragment CB5 by mild acid hydrolysis, by trypsin and chymotrypsin.

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