Protein interactions near crystallization: a microscopic approach to the Hofmeister series

被引:60
作者
Piazza, R [1 ]
Pierno, M
机构
[1] Ist Nazl Fis Mat, Unit Pavia, Milan, Italy
[2] Politecn Milan, Dipartimento Ingn Nucl, I-20133 Milan, Italy
关键词
D O I
10.1088/0953-8984/12/8A/361
中图分类号
O469 [凝聚态物理学];
学科分类号
070205 ;
摘要
The salting-out effect of simple electrolytes on lysozyme has been studied by measuring the second virial coefficient B-2 Of the osmotic pressure as a function of salt concentration, and for different salts. The aim of this work has been to End a microscopic counterpart of the empirical Hofmeister series for the efficiency of cations and anions in inducing protein crystallization. The experimental results show that, for large enough ionic strengths, B-2 scales linearly with the salt concentration. This trend is common to a number of different monovalent salts, however with efficiency strongly dependent on the specific anion. Conversely, changing the cation does not appreciably affect B-2. The significance of these findings for the investigation-of protein interactions near crystallization is discussed.
引用
收藏
页码:A443 / A449
页数:7
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