Why the properties of proteins in salt solutions follow a Hofmeister series

被引：63

作者：

Boström, M

Williams, DRM

Ninham, BW

机构：

[1] Linkoping Univ, Dept Phys & Measurement Technol, SE-58183 Linkoping, Sweden

[2] Inst Adv Studies, Res Sch Phys Sci & Engn, Canberra, ACT 0200, Australia

[3] Univ Florence, Dept Chem, I-50121 Florence, Italy

[4] Univ Regensburg, Dept Chem, D-8400 Regensburg, Germany

来源：

CURRENT OPINION IN COLLOID & INTERFACE SCIENCE | 2004年 / 9卷 / 1-2期

关键词：

Hofmeister effect; ionic dispersion forces; lysozyme; salt solution;

D O I：

10.1016/j.cocis.2004.05.001

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：

The physical properties of hen-egg-white lysozyme, and other globular protein, in aqueous solutions depend in a complicated and unexplained way on pH, salt type and salt concentration. One important and previously neglected source of ion specificity is the ionic dispersion potential that acts between each ion and the protein. We present model calculations, performed within a modified ion-specific double layer theory, that demonstrate the large effect of including these ionic dispersion potentials. (C) 2004 Elsevier Ltd. All rights reserved.

引用

页码：48 / 52

页数：5

共 28 条

[1] Role of Co-Ion specificity and dissolved atmospheric gas in colloid interaction [J].