The Hofmeister effect as seen by SAXS in protein solutions

被引：92

作者：

Finet, S

Skouri-Panet, F

Casselyn, M

Bonneté, F

Tardieu, A

机构：

[1] Univ Paris 06, CNRS, LMCP, F-75252 Paris 05, France

[2] European Synchrotron Radiat Facil, F-38043 Grenoble, France

[3] Bioinformat Struct Ctr Genet Mol, F-91198 Gif Sur Yvette, France

[4] Univ Aix Marseille 2, CNRS, CRMCN, F-13288 Marseille 09, France

[5] Univ Aix Marseille 3, CNRS, CRMCN, F-13288 Marseille 09, France

来源：

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

关键词：

Hofmeister series; biological macromolecules; solution interactions; small angle X-ray scattering;

D O I：

10.1016/j.cocis.2004.05.014

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 interactions in solution are conveniently analysed with small angle X-ray scattering (SAXS). Such an analysis has shown that the addition of monovalent salt induces an additional attraction between macromolecules. A differential effect of the anions is observed, which follows the order of the Hofmeister series. Such experimental observations should be helpful to test the adequacy of theoretical models. (C) 2004 Elsevier Ltd. All rights reserved.

引用

收藏

页码：112 / 116

页数：5

相关论文

共 28 条

[1] ELECTROSTATIC INTERACTIONS IN COLLOIDAL SOLUTIONS - COMPARISON BETWEEN PRIMITIVE AND ONE-COMPONENT MODELS [J].

BELLONI, L .

JOURNAL OF CHEMICAL PHYSICS, 1986, 85 (01) :519-526

[2] Attraction of electrostatic origin between colloids [J].

Belloni, L ;

Spalla, O .

JOURNAL OF CHEMICAL PHYSICS, 1997, 107 (02) :465-480

[3] Interest of the normalized second virial coefficient and interaction potentials for crystallizing large macromolecules [J].

Bonneté, F ;

Vivarès, D .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2002, 58 :1571-1575

[4] Different tools to study interaction potentials in gamma-crystallin solutions: Relevance to crystal growth [J].

Bonnete, F ;

Malfois, M ;

Finet, S ;

Tardieu, A ;

Lafont, S ;

Veesler, S .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1997, 53 :438-447

[5] Second virial coefficient:: variations with lysozyme crystallization conditions [J].

Bonneté, F ;

Finet, S ;

Tardieu, A .

JOURNAL OF CRYSTAL GROWTH, 1999, 196 (2-4) :403-414

[6] Special ion effects:: Why the properties of lysozyme in salt solutions follow a Hofmeister series [J].

Boström, M ;

Williams, DRM ;

Ninham, BW .

BIOPHYSICAL JOURNAL, 2003, 85 (02) :686-694

[7] BINARY-LIQUID PHASE-SEPARATION OF LENS PROTEIN SOLUTIONS [J].

BROIDE, ML ;

BERLAND, CR ;

PANDE, J ;

OGUN, OO ;

BENEDEK, GB .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (13) :5660-5664

[8] Interactions in solution of a large oligomeric protein [J].

Budayova, M ;

Bonneté, F ;

Tardieu, A ;

Vachette, P .

JOURNAL OF CRYSTAL GROWTH, 1999, 196 (2-4) :210-219

[9] Spherical plant viruses: interactions in solution, phase diagrams and crystallization of brome mosaic virus [J].

Casselyn, M ;

Perez, J ;

Tardieu, A ;

Vachette, P ;

Witz, J ;

Delacroix, H .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2001, 57 :1799-1812

[10] SHORT-RANGE ORDER OF CRYSTALLIN PROTEINS ACCOUNTS FOR EYE LENS TRANSPARENCY [J].

DELAYE, M ;

TARDIEU, A .

NATURE, 1983, 302 (5907) :415-417