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Titolo:
Protein folding: Looping from hydrophobic nuclei
Autore:
Berezovsky, IN; Kirzhner, VM; Kirzhner, A; Trifonov, EN;
Indirizzi:
Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 ruct, IL-76100 Rehovot, Israel Univ Haifa, Inst Evolut, Genome Divers Ctr, IL-31999 Haifa, Israel Univ Haifa Haifa Israel IL-31999 nome Divers Ctr, IL-31999 Haifa, Israel
Titolo Testata:
PROTEINS-STRUCTURE FUNCTION AND GENETICS
fascicolo: 4, volume: 45, anno: 2001,
pagine: 346 - 350
SICI:
0887-3585(200112)45:4<346:PFLFHN>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLOBULAR-PROTEINS;
Keywords:
protein folding; closed loops; nuclei; hydrophobicity; domains; complete genomes; major folds;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
16
Recensione:
Indirizzi per estratti:
Indirizzo: Berezovsky, IN Weizmann Inst Sci, Dept Biol Struct, POB 26, IL-76100 Rehovot, Israel Weizmann Inst Sci POB 26 Rehovot Israel IL-76100 t, Israel
Citazione:
I.N. Berezovsky et al., "Protein folding: Looping from hydrophobic nuclei", PROTEINS, 45(4), 2001, pp. 346-350

Abstract

Protein structure can be viewed as a compact linear array of nearly standard size closed loops of 25-30 amino acid residues (Berezovsky et al., FEBS Letters 2000; 466: 283-286) irrespective of details of secondary structure. The end-to-end contacts in the loops are likely to be hydrophobic, which is a testable hypothesis. This notion could be verified by direct comparisonof the loop maps with Kyte and Doolittle hydropathicity plots. This analysis reveals that most of the ends of the loops are hydrophobic, indeed. The same conclusion is reached on the basis of positional autocorrelation analysis of protein sequences of 23 fully sequenced bacterial genomes. Hydrophobic residues valine, alanine, glycine, leucine, and isoleucine appear preferentially at the 25-30 residues distance one from another. These observations open a new perspective in the understanding of protein structure and folding: a consecutive looping of the polypeptide chain with the loops ending primarily at hydrophobic nuclei. (C) 2001 Wiley-Liss, Inc.

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Documento generato il 25/09/20 alle ore 00:01:52