著者

水野 元博 宮東 達也 新屋 隆士

出版者

日本結晶成長学会

雑誌

日本結晶成長学会誌 (ISSN:03856275)

巻号頁・発行日

vol.42, no.4, pp.268-273, 2016 (Released:2017-05-31)

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For hydrated proteins, hydration waters largely contribute to the structure and properties of proteins. Therefore, the information of the dynamics of hydration waters in proteins is very important for understanding unique structure, function and crystal growth of protein. In the present study, the change in the rotational motion of water molecules around dynamical transition point (T_D〜220 K) was investigated for hydrated lysozyme using solid-state ^2H NMR. An Arrhenius-type temperature dependence of correlation time for the rotational motion of water molecules was observed above and below T_D. Although the water molecules at the surface of proteins undergo fast isotropic rotation above T_D, 180° flip becomes main motion of water molecules below T_D. Thus, the dynamics of hydrated water is found to be suppressed below T_D. The large distribution of the electric field gradient at ^2H observed below T_D indicates the glassy state of hydration water in protein.