Informatics on hydration structures of proteis

蛋白质的水化作用是研究蛋白质功能、折叠和动力学的重要课题之一。在研究蛋白质水化结构的众多技术中，低温X射线结晶学和分子动力学模拟为蛋白质水化提供了大量的信息。在这个项目中，我研究了蛋白质水化结构的静态和动态特性。特别是，在谷氨酸脱氢酶的晶体结构分析中，我观察到了水化结构变化和结构域运动的动态耦合。这是第一个揭示蛋白质运动中这种耦合的实验证据。此外，我还研究了人溶菌酶在160K左右发生的玻璃化转变。通过对蛋白质的分子动力学模拟，我们发现了水偶极子在蛋白质表面的选择性取向。本研究的结果可能为蛋白质在水溶液中的动态和折叠提供新的见解。

Hydration of protein is one of the most important subjects to study the function, folding and dynamics of the protein. Among many techniques investigating hydration structures of proteins, cryogenic X-ray crystallography and molecular dynamics simulation have provided much information on protein hydration. In this project, I studied the static and dynamical characteristics of hydration structures of proteins. In particular, in the crystal structure analysis of glutamate dehydrogenase, I observed the dynamical coupling of hydration structural changes and the domain motion. This is the first experimental evidence to reveals such coupling in protein motion. In addition I investigated the glassy transition occurring around 160 K for human lysozyme. Through molecular dynamics simulations of proteins, we found the selective orientation of water dipoles on the surface of proteins. The results of the present research may provide new insights into the dynamics and folding of proteins in aqueous solution.