The Hofmeister series and protein-salt interactions

被引:82
作者
Shimizu, Seishi [1 ]
McLaren, William M.
Matubayasi, Nobuyuki
机构
[1] Univ York, Dept Chem, York Struct Biol Lab, York YO10 5YW, N Yorkshire, England
[2] Kyoto Univ, Inst Chem Res, Kyoto 6110011, Japan
基金
日本学术振兴会; 英国生物技术与生命科学研究理事会;
关键词
D O I
10.1063/1.2206174
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
In order to understand the origin of the Hofmeister series, a statistical-mechanical analysis, based upon the Kirkwood-Buff (KB) theory, has been performed to extract information regarding protein hydration and water-mediated protein-salt interactions from published experimental data-preferential hydration and volumetric data for bovine serum albumin in the presence of a wide range of salts. The analysis showed a linear correlation between the preferential hydration parameter and the protein-cosolvent KB parameter. The same linear correlation holds even when nonelectrolyte cosolvents, such as polyethelene glycol, have been incorporated. These results suggest that the Hofmeister series is due to a wide variation of the water-mediated protein-cosolvent interaction (but not the change of protein hydration) and that this mechanism is a special case of a more general scenario common even to the macromolecular crowding. (c) 2006 American Institute of Physics.
引用
收藏
页数:4
相关论文
共 34 条
[1]   WHY PREFERENTIAL HYDRATION DOES NOT ALWAYS STABILIZE THE NATIVE STRUCTURE OF GLOBULAR-PROTEINS [J].
ARAKAWA, T ;
BHAT, R ;
TIMASHEFF, SN .
BIOCHEMISTRY, 1990, 29 (07) :1924-1931
[2]   PROTEIN STABILIZATION AND DESTABILIZATION BY GUANIDINIUM SALTS [J].
ARAKAWA, T ;
TIMASHEFF, SN .
BIOCHEMISTRY, 1984, 23 (25) :5924-5929
[3]   MECHANISM OF PROTEIN SALTING IN AND SALTING OUT BY DIVALENT-CATION SALTS - BALANCE BETWEEN HYDRATION AND SALT BINDING [J].
ARAKAWA, T ;
TIMASHEFF, SN .
BIOCHEMISTRY, 1984, 23 (25) :5912-5923
[4]   PREFERENTIAL INTERACTIONS DETERMINE PROTEIN SOLUBILITY IN 3-COMPONENT SOLUTIONS - THE MGCL2 SYSTEM [J].
ARAKAWA, T ;
BHAT, R ;
TIMASHEFF, SN .
BIOCHEMISTRY, 1990, 29 (07) :1914-1923
[5]   How Hofmeister ion interactions affect protein stability [J].
Baldwin, RL .
BIOPHYSICAL JOURNAL, 1996, 71 (04) :2056-2063
[6]  
Ben-Naim A., 1992, STAT THERMODYNAMICS, P372
[7]  
Chan HS, 2004, METHOD ENZYMOL, V380, P350
[8]   Preferential interactions of cosolvents with hydrophobic solutes [J].
Chitra, R ;
Smith, PE .
JOURNAL OF PHYSICAL CHEMISTRY B, 2001, 105 (46) :11513-11522
[9]   THE HOFMEISTER EFFECT AND THE BEHAVIOR OF WATER AT INTERFACES [J].
COLLINS, KD ;
WASHABAUGH, MW .
QUARTERLY REVIEWS OF BIOPHYSICS, 1985, 18 (04) :323-422
[10]   Interpreting the effects of small uncharged solutes on protein-folding equilibria [J].
Davis-Searles, PR ;
Saunders, AJ ;
Erie, DA ;
Winzor, DJ ;
Pielak, GJ .
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 2001, 30 :271-306