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Auteur E. N. Trifonov
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Faire une suggestion Affiner la rechercheEvolutionary Aspects of Protein Structure and Folding / I. N. Berezovsky
Titre : Evolutionary Aspects of Protein Structure and Folding Type de document : articles et extraits Auteurs : I. N. Berezovsky, Auteur ; E. N. Trifonov, Auteur Année de publication : 2001 Importance : p.233-239 Langues : Français (fre) Mots-clés : Folding mechanism Protein evolution Résumé : Four basic stages of evolution of protein structure are described, basing on recent work of the authors aimed specifically to reconstruct the earliest events in the protein evolution. According to this reconstruction, the initial stage of short peptides comprising, probably, only a few amino acid residues had been followed by formation of closed loops of 25–30 residues, which corresponds to the polymer-statistically optimal ring closure size for mixed polypeptide chains. The next stage involved fusion of relatively small linear genes and formation of protein structures consisting of several closed loops of a nearly standard size, with 4–6 loops (100–200 amino acid residues) in a typical protein fold. The last, modern stage began with combinatorial fusion of the presumably circular 300–600 bp DNA units and, accordingly, formation of multidomain proteins.
Evolutionary Aspects of Protein Structure and Folding [articles et extraits] / I. N. Berezovsky, Auteur ; E. N. Trifonov, Auteur . - 2001 . - p.233-239.
Langues : Français (fre)
Mots-clés : Folding mechanism Protein evolution Résumé : Four basic stages of evolution of protein structure are described, basing on recent work of the authors aimed specifically to reconstruct the earliest events in the protein evolution. According to this reconstruction, the initial stage of short peptides comprising, probably, only a few amino acid residues had been followed by formation of closed loops of 25–30 residues, which corresponds to the polymer-statistically optimal ring closure size for mixed polypeptide chains. The next stage involved fusion of relatively small linear genes and formation of protein structures consisting of several closed loops of a nearly standard size, with 4–6 loops (100–200 amino acid residues) in a typical protein fold. The last, modern stage began with combinatorial fusion of the presumably circular 300–600 bp DNA units and, accordingly, formation of multidomain proteins.
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Code-barres Cote Support Localisation Section Disponibilité ART-6910-0 ART Document imprimé Bureau chercheur Bureau de FRISCH, Thomas Disponible Journal of biomolecular structure and dynamics, Vol.20 No.1. Loop Fold Structure of Proteins : Resolution of Levinthal’s Paradox / I. N. Berezovsky
in Journal of biomolecular structure and dynamics (JBSD)
Titre de série : Journal of biomolecular structure and dynamics, Vol.20 No.1 Titre : Loop Fold Structure of Proteins : Resolution of Levinthal’s Paradox Type de document : articles et extraits Auteurs : I. N. Berezovsky, Auteur ; E. N. Trifonov, Auteur Année de publication : 2002 Importance : p.5-6 ISBN/ISSN/EAN : 0739-1102 Langues : Français (fre) Résumé : According to Levinthal a protein chain of ordinary size would require enormous time to sort its conformational states before the final fold is reached. Experimentally observed time of folding suggests an estimate of the chain length for which the time would be sufficient. This estimate by order of magnitude fits to experimentally observed universal closed loop elements of globular proteins –25-30 residues. Key words: Levinthal’s paradox, protein folding, chain conformation, closed loops, loop fold structure
in Journal of biomolecular structure and dynamics (JBSD)
Journal of biomolecular structure and dynamics, Vol.20 No.1. Loop Fold Structure of Proteins : Resolution of Levinthal’s Paradox [articles et extraits] / I. N. Berezovsky, Auteur ; E. N. Trifonov, Auteur . - 2002 . - p.5-6.
ISSN : 0739-1102
Langues : Français (fre)
Résumé : According to Levinthal a protein chain of ordinary size would require enormous time to sort its conformational states before the final fold is reached. Experimentally observed time of folding suggests an estimate of the chain length for which the time would be sufficient. This estimate by order of magnitude fits to experimentally observed universal closed loop elements of globular proteins –25-30 residues. Key words: Levinthal’s paradox, protein folding, chain conformation, closed loops, loop fold structure
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Code-barres Cote Support Localisation Section Disponibilité ART-6916-0 ART Document imprimé Bureau chercheur Bureau de FRISCH, Thomas Disponible Molecular biology, Vol.25 No.2. Evolutionary aspects of protein structure and folding / I. N. Berezovsky
in Molecular Biology
Titre de série : Molecular biology, Vol.25 No.2 Titre : Evolutionary aspects of protein structure and folding Type de document : articles et extraits Auteurs : I. N. Berezovsky, Auteur ; E. N. Trifonov, Auteur Année de publication : 2001 Importance : p.233-239 ISBN/ISSN/EAN : 0026-8933 Langues : Français (fre)
in Molecular Biology
Molecular biology, Vol.25 No.2. Evolutionary aspects of protein structure and folding [articles et extraits] / I. N. Berezovsky, Auteur ; E. N. Trifonov, Auteur . - 2001 . - p.233-239.
ISSN : 0026-8933
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Code-barres Cote Support Localisation Section Disponibilité ART-6922-0 ART Document imprimé Bureau chercheur Bureau de FRISCH, Thomas Disponible Protein Engineering, Vol.15 No.12. Closed loops: persistence of the protein chain returns / I. N. Berezovsky
in Protein Engineering
Titre de série : Protein Engineering, Vol.15 No.12 Titre : Closed loops: persistence of the protein chain returns Type de document : articles et extraits Auteurs : I. N. Berezovsky, Auteur ; A. Kirzhner, Auteur ; V. M. Kirzhner, Auteur ; V. Rosenfeld, Auteur ; E. N. Trifonov, Auteur Année de publication : 2002 Importance : p.955-957 Langues : Français (fre) Résumé : It has recently been discovered that globular proteins are universally built from standard loop-n-lock units of about 30 amino acid residues. The hypothesis has been put forward on the loop stage in the protein evolution when the units were autonomous. Later they joined together making longer chains. One would expect that the early individual loop-n-lock elements might still be detected in modern protein sequences as remnants of the hypothetical 30-residue sequence prototypes. Among several strong sequence motifs, extracted from protein sequences of 23 complete bacterial proteomes, one 32-residue prototype was studied here in detail. Numerous sequence segments related to the prototype are identified in the crystal structures of proteins of a PDB_SELECT database. Analysis of the respective chain trajectories for the cases with different degrees of sequence conservation confirms that the majority of the segments correspond to the closed loops. In the evolutionary diversification of the prototypes the secondary structure yields first, while the sequence is still moderately conserved. The last feature to go is the chain return property. Apparently, the opening of the loops would severely destabilize the protein fold, which explains their conservation.
in Protein Engineering
Protein Engineering, Vol.15 No.12. Closed loops: persistence of the protein chain returns [articles et extraits] / I. N. Berezovsky, Auteur ; A. Kirzhner, Auteur ; V. M. Kirzhner, Auteur ; V. Rosenfeld, Auteur ; E. N. Trifonov, Auteur . - 2002 . - p.955-957.
Langues : Français (fre)
Résumé : It has recently been discovered that globular proteins are universally built from standard loop-n-lock units of about 30 amino acid residues. The hypothesis has been put forward on the loop stage in the protein evolution when the units were autonomous. Later they joined together making longer chains. One would expect that the early individual loop-n-lock elements might still be detected in modern protein sequences as remnants of the hypothetical 30-residue sequence prototypes. Among several strong sequence motifs, extracted from protein sequences of 23 complete bacterial proteomes, one 32-residue prototype was studied here in detail. Numerous sequence segments related to the prototype are identified in the crystal structures of proteins of a PDB_SELECT database. Analysis of the respective chain trajectories for the cases with different degrees of sequence conservation confirms that the majority of the segments correspond to the closed loops. In the evolutionary diversification of the prototypes the secondary structure yields first, while the sequence is still moderately conserved. The last feature to go is the chain return property. Apparently, the opening of the loops would severely destabilize the protein fold, which explains their conservation.
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Code-barres Cote Support Localisation Section Disponibilité ART-6919-0 ART Document imprimé Bureau chercheur Bureau de FRISCH, Thomas Disponible