Hydrophobic forces between protein molecules in aqueous solutions of concentrated electrolyte

被引:66
作者
Curtis, RA
Steinbrecher, C
Heinemann, A
Blanch, HW [1 ]
Prausnitz, JM
机构
[1] Univ Calif Berkeley, Dept Chem Engn, Berkeley, CA 94720 USA
[2] Univ Calif Berkeley, Lawrence Berkeley Lab, Div Chem Sci, Berkeley, CA 94720 USA
基金
美国国家科学基金会;
关键词
intermolecular interactions; potentials of mean force; lysozyme; salting-out; salts; hydrophobic effect;
D O I
10.1016/S0301-4622(02)00071-6
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
Protein-protein interactions have been measured for a mutant (D101F) lysozyme and for native lysozyme in concentrated solutions of ammonium sulfate at pH 7 and sodium chloride at pH 4.5. In the mutant lysozyme, a surface aspartate residue has been replaced with a hydrophobic phenylalanine residue. The protein-protein interactions of D101F lysozyme are more attractive than those of native lysozyme for all conditions studied. The salt-induced attraction is correlated with a solvation potential of mean force given by the work required to desolvate the part of the protein surfaces that is buried by the protein-protein interaction. This work is proportional to the aqueous surface-tension increment of the salt and the fractional non-polar surface coverage of the protein. Experimental measurements of osmotic second virial coefficients validate a proposed potential of mean force that ascribes the salt-induced attraction between protein molecules to an enhancement of the hydrophobic attraction. This model provides a first approximation for predicting the protein-protein potential of mean force in concentrated aqueous electrolyte solutions; this potential is useful for determining solution conditions favorable for protein crystallization. (C) 2002 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:249 / 265
页数:17
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