Informatics on hydration structures of proteis

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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.