Hofmeister effects:: Why protein charge, pH titration and protein precipitation depend on the choice of background salt solution

被引:57
|
作者
Moreira, L. A.
Bostrom, M.
Ninham, B. W. [1 ]
Biscaia, E. C.
Tavares, F. W.
机构
[1] Australian Natl Univ, Res Sch Phys Sci & Engn, Dept Appl Math, Canberra, ACT 0200, Australia
[2] Fed Univ Rio De Janeiro, Escola Quim, BR-21949900 Rio De Janeiro, RJ, Brazil
[3] Linkoping Univ, Dept Phys & Measurement Technol, SE-58183 Linkoping, Sweden
[4] Fed Univ Rio De Janeiro, COPPE, Programa Engn Quim, BR-21945970 Rio De Janeiro, RJ, Brazil
关键词
Hofmeister effect; polarizability; ionic dispersion potentials; cytochrome C; Poisson-Boltzmann equation;
D O I
10.1016/j.colsurfa.2005.11.021
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
Protein solubility, protein charge and acid-base titration in protein solutions depend strongly on the choice of background salt solution. Hofmeister effects, or sequences, refer to the relative effectiveness of anions or cations on a wide range of phenomena. Understanding this ion specificity is vital for biology, biotechnology, and colloid chemistry but the reason has. until very recently, not been clear. We present calculations using the Poisson-Boltzmann equation that includes not only electrostatic interactions but also many-body ion-protein dispersion potentials, originated from polarizabilities of ions and proteins. These calculations reveal that is possible to qualitatively predict different Hofmeister effects observed in protein solutions. Our results enable us to give an explanation for the Hofmeister series observed in the measured pH in protein and buffer solutions, protein charge and ion adsorption on protein surface. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码:457 / 463
页数:7
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