A computer simulation study of water drying at the interface of protein chains
A computer simulation study of water drying at the interface of protein chains
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DOI：
10.1063/1.1766017
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发表时间：
2004-07-22
影响因子：
4.4
通讯作者：
Chen, CL
中科院分区：
文献类型：
--
作者：
Huang, Q;Ding, SW;Chen, CL
本研究通过使用显式水表示的纳秒分子动力学模拟，研究了二聚蛋白两条链界面区域的水干燥（空化）。在该区域直接观察到分离引起的水空腔。我们评估了发生干燥转变的两条链的分离长度尺度，以及转变期间从界面区域排出的水分子的平均数量。所获得的值可以通过限制横向尺寸有限的开尔文方程来合理化[K. Lum 和 A. Luzar，物理学家。修订版 E 56，R6283 (1997)]。此外，我们发现干燥转变伴随着每个界面水分子的平均氢键数呈指数减少。这项研究的结果可能会加深对疏水相互作用如何驱动蛋白质链组装的理解。 (C) 2004 年美国物理研究所。
This study investigated the water drying (cavitation) in the interfacial region of two chains of a dimeric protein by nanosecond molecular dynamics simulations using explicit water representation. Separation-induced cavity of water was directly observed in the region. We evaluated the separation length scale of two chains on which the drying transition occurs, and the average number of water molecules that are expelled from the interfacial region during the transition. The obtained values can be rationalized by Kelvin equation for finite lateral size of confinement [K. Lum and A. Luzar, Phys. Rev. E 56, R6283 (1997)]. Also, we found that the drying transition is accompanied by an exponential reduction in the average hydrogen-bond number per interfacial water molecule. The results of this study may deepen the understanding of how hydrophobic interaction drives the assembly of protein chains. (C) 2004 American Institute of Physics.