A model for the thermodynamics of globular proteins

被引：7
|
作者：
Hansen, A [1 ]
Jensen, MH
Sneppen, K
Zocchi, G
机构：
[1] Norwegian Univ Sci & Technol, NTNU, Dept Phys, N-7034 Trondheim, Norway
[2] Niels Bohr Inst, DK-2100 Copenhagen O, Denmark
[3] NORDITA, DK-2100 Copenhagen O, Denmark
来源：
PHYSICA A | 1999年 / 270卷 / 1-2期
关键词：
protein folding; protein thermodynamics; cold denaturation; folding pathways;
D O I：
10.1016/S0378-4371(99)00131-4
中图分类号：
O4 [物理学];
学科分类号：
0702 ;
摘要：
We review a statistical mechanics treatment of the stability of globular proteins based on a simple model Hamiltonian taking into account protein self-interactions and protein-water interactions. The model contains both hot and cold folding transitions. In addition it predicts a critical point at a given temperature and chemical potential of the sur rounding water. The universality class of this critical point is new. (C) 1999 Published by Elsevier Science B.V. All rights reserved.
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页码：278 / 287
页数：10
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