Evidence for non-DLVO hydration interactions in solutions of the protein apoferritin

被引:128
|
作者
Petsev, DN [1 ]
Vekilov, PG
机构
[1] Univ Alabama, Ctr Micrograv & Mat Res, Huntsville, AL 35899 USA
[2] Univ Alabama, Dept Chem, Huntsville, AL 35899 USA
关键词
D O I
10.1103/PhysRevLett.84.1339
中图分类号
O4 [物理学];
学科分类号
0702 ;
摘要
We have studied molecular interactions in solutions of the protein apoferritin by static and dynamic light scattering. When plotted against the electrolyte concentration, the second osmotic virial coefficient exhibits a minimum. The ascending branch of this dependence is a manifestation of a surprisingly strong repulsion between the molecules at electrolyte concentrations about and above 0.2M, where electrostatic interactions are suppressed. We argue that the repulsion is due to the water structuring, enhanced by the accumulation of hydrophilic counterions around the apoferritin molecules, giving rise to so-called hydration forces.
引用
收藏
页码:1339 / 1342
页数:4
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