On the cold denaturation of globular proteins

被引：15

作者：

Ascolese, Eduardo ^{[1
]}

Graziano, Giuseppe ^{[1
]}

机构：

[1] Univ Sannio, Dipartimento Sci Biol & Ambientali, I-82100 Benevento, Italy

来源：

CHEMICAL PHYSICS LETTERS | 2008年 / 467卷 / 1-3期

关键词：

D O I：

10.1016/j.cplett.2008.10.078

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The recent finding that yeast frataxin shows, at pH 7.0, cold denaturation at 274 K and hot denaturation at 303 K [A. Pastore, S. R. Martin, A. Politou, K. C. Kondapalli, T. Stemmler, P. A. Temussi, J. Am. Chem. Soc. 129 (2007) 5374] calls for a deeper rationalization of the molecular mechanisms stabilizing-destabilizing the native state of globular proteins. It is shown that the statistical thermodynamic model originally developed by Ikegami can reproduce in a more-than-qualitative manner the two conformational transitions of yeast frataxin, providing important clues on their molecular origin. (C) 2008 Elsevier B.V. All rights reserved.

引用

页码：150 / 153

页数：4

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