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.

引用

页码：278 / 287

页数：10

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