Relaxational dynamics of water molecules at protein surface

被引：96

作者：

Dellerue, S ^{[1
]}

Bellissent-Funel, MC ^{[1
]}

机构：

[1] CEA Saclay, CNRS, Leon Brillouin Lab, CEA, F-91191 Gif Sur Yvette, France

来源：

CHEMICAL PHYSICS | 2000年 / 258卷 / 2-3期

关键词：

D O I：

10.1016/S0301-0104(00)00181-6

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：

Relaxational dynamics of water molecules at the surface of a C-phycocyanin protein is studied by high resolution quasi-elastic neutron scattering. The neutron quasi-elastic spectra are well described by the alpha-relaxation process of mode coupling theory of supercooled liquids. The relaxation times of interfacial water exhibit a power law dependence on the wave vector Q. The average diffusion coefficient is 10 times lower than that of bulk water. This confirms that there is a retardation of water molecules at the protein surface which is in good agreement with the results of water at the surface of hydrophilic model systems. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：315 / 325

页数：11

共 60 条

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