Thermodynamic relationships between protein-solvent and protein-protein interactions

被引:11
作者
Costenaro, L [1 ]
Ebel, C [1 ]
机构
[1] UJF, CEA, Inst Biol Struct, Lab Biophys Mol,CNRS,UMR 5075, F-38027 Grenoble, France
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷
关键词
solvent; interactions; thermodynamics; hydration; solubility; binding; second virial coefficient;
D O I
10.1107/S0907444902014397
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
How the solvent modulates the weak inter-particle interactions in solution and affects macromolecule solubility is not yet understood. Well-established thermodynamic relationships link second virial coefficient and preferential solute binding parameter. We present the meaning of these thermodynamic parameters and the way to measure them. When a solvation shell has a composition different from the bulk solvent, a negative contribution is found in the second virial coefficient corresponding to an effective attraction between the macromolecules in solution. A quantitative evaluation using simple models of solvated particles in solution suggests that solvation could induce, at high or low concentration of a small molecule solute, attractive inter-particle interactions corresponding to favorable crystallization conditions.
引用
收藏
页码:1554 / 1559
页数:6
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