Effect of Nonadditive Repulsive Intermolecular Interactions on the Light Scattering of Concentrated Protein-Osmolyte Mixtures

被引：17

作者：

Fernandez, Cristina ^{[1
]}

Minton, Allen P. ^{[1
]}

机构：

[1] NIDDK, Sect Phys Biochem, Lab Biochem & Genet, NIH,US Dept Hlth & Human Serv, Bethesda, MD 20892 USA

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2011年 / 115卷 / 05期

关键词：

BOVINE SERUM-ALBUMIN; HARD PARTICLE MODEL; SELF-ASSOCIATING PROTEINS; OSMOTIC-PRESSURE;

D O I：

10.1021/jp110285b

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 static light scattering of three globular proteins; bovine serum albumin, ovalbumin, and ovomucoid, and binary mixtures of each protein and trimethylamine oxide (TMAO) containing between 10 and 70% protein, Were measured as a function of total weight per volume concentration up to 100 g/L. The observed dependence of scattering upon concentration may be accounted for quantitatively by an effective hard sphere model incorporating an extension that takes into account the nonadditive nature of the repulsive intermolecular interaction between protein and TMAO.

引用

收藏

页码：1289 / 1293

页数：5

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