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Titolo:
Molecular dynamics simulations of urea and thermal-induced denaturation ofS-peptide analogue
Autore:
Zhang, ZY; Zhu, YJ; Shi, YY;
Indirizzi:
Univ Sci & Technol China, Sch Life Sci, Struct Biol Lab, Hefei 230026, Anhui, Peoples R China Univ Sci & Technol China Hefei Anhui Peoples R China 230026 oples R China
Titolo Testata:
BIOPHYSICAL CHEMISTRY
fascicolo: 2-3, volume: 89, anno: 2001,
pagine: 145 - 162
SICI:
0301-4622(20010215)89:2-3<145:MDSOUA>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
MACROMOLECULAR STRUCTURES; GUANIDINIUM CHLORIDE; SOLVENT DENATURATION; AQUEOUS UREA; PROTEINS; BINDING; WATER; MODEL; STABILIZATION; SOLVATION;
Keywords:
molecular dynamics; denaturation; hydrophobic effects; hydrogen bonds; cluster analysis; essential dynamics analysis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Shi, YY Univ Sci & Technol China, Sch Life Sci, Struct Biol Lab, Hefei 230026, Anhui, Peoples R China Univ Sci & Technol China Hefei Anhui Peoples RChina 230026 China
Citazione:
Z.Y. Zhang et al., "Molecular dynamics simulations of urea and thermal-induced denaturation ofS-peptide analogue", BIOPHYS CH, 89(2-3), 2001, pp. 145-162

Abstract

Molecular dynamics simulations of the S-peptide analogue AETAAAKFLREHMDS in water at 278 and 358 K, and in 8 M urea at 278 K were performed. The results show agreement with experiments. The helix is stable at low temperature(278 K), while at 358 K, unfolding is observed. The effects of urea on protein stability have been studied. The data support a model in which urea denatures proteins by: (I) diminishing the hydrophobic effect by displacing water molecules from the solvent shell around nonpolar groups; and (2) binding directly to amide units (NH and CO groups) via hydrogen bonds. The results of cluster analysis and essential dynamics analysis suggest that the mechanism of urea and thermal-induced denaturation may not be the same. (C) 2001 Elsevier Science B.V. All rights reserved.

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Documento generato il 25/01/20 alle ore 16:37:07