共 31 条
[31]
WETLAUFER DB, 1964, J AM CHEM SOC, V86, P508
Protein volume changes on cosolvent denaturation
被引：17
作者：
Smith, PE
[1
]
机构：
[1] Kansas State Univ, Dept Chem, Manhattan, KS 66506 USA
基金：
美国国家科学基金会;
关键词：
protein volume;
cosolvent;
protein denaturation;
protein aggregation;
preferential interactions;
D O I：
10.1016/j.bpc.2004.10.002
中图分类号：
Q5 [生物化学];
Q7 [分子生物学];
学科分类号：
071010 ;
081704 ;
摘要：
A thermodynamic relationship is obtained which links the effect of a cosolvent on the denaturation equilibrium of a protein to the effect of the cosolvent on the change in partial molar volume (pmv) of a protein on denaturation. The relationship uses the concept of preferential interactions and is exact for an infinitely dilute protein. Analysis of the literature data on protein volume changes suggests that many of the observed volume changes are thermodynamically inconsistent with the corresponding free energy changes, especially at low cosolvent concentrations. It is argued that the most reasonable explanation for this involves cosolvent induced changes in the degree of protein-protein association. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码：299 / 302
页数：4
相关论文