Relaxational dynamics of water molecules at protein surface
Relaxational dynamics of water molecules at protein surface
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DOI：
10.1016/s0301-0104(00)00181-6
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发表时间：
2000-08-15
期刊：
影响因子：
2.3
通讯作者：
Bellissent-Funel, MC
中科院分区：
文献类型：
--
作者：
Dellerue, S;Bellissent-Funel, MC
用高分辨准弹性中子散射研究了水分子在藻蓝蛋白表面的弛豫动力学。中子准弹性能谱可用过冷液体模式耦合理论的α弛豫过程来描述。界面水的弛豫时间与波矢Q呈幂律关系。平均扩散系数比本体水低10倍。这证实了在蛋白质表面存在水分子的阻滞，这与亲水性模型系统表面的水的结果非常一致。(C)2000 Elsevier Science B.V.保留所有权利。
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.