Freezable and Unfreezable Hydration Water: Distinct Contributions to Protein Dynamics Revealed by Neutron Scattering

被引:10
作者
Yamamoto, Naoki [2 ]
Kofu, Maiko [1 ]
Nakajima, Kenji [1 ]
Nakagawa, Hiroshi [1 ]
Shibayama, Naoya [2 ]
机构
[1] Japan Atom Energy Agcy, J PARC Ctr, Ibaraki 3191195, Japan
[2] Jichi Med Univ, Dept Physiol, Div Biophys, Shimotsuke, Tochigi 3290498, Japan
关键词
BAND DIELECTRIC-SPECTROSCOPY; GLASS-TRANSITION; TEMPERATURE; MOTIONS;
D O I
10.1021/acs.jpclett.0c03786
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Hydration water plays a crucial role for activating the protein dynamics required for functional expression. Yet, the details are not understood about how hydration water couples with protein dynamics. A temperature hysteresis of the ice formation of hydration water is a key phenomenon to understand which type of hydration water, unfreezable or freezable hydration water, is crucial for the activation of protein dynamics. Using neutron scattering, we observed a temperature-hysteresis phenomenon in the diffraction peaks of the ice of freezable hydration water, whereas protein dynamics did not show any temperature hysteresis. These results show that the protein dynamics is not coupled with freezable hydration water dynamics, and unfreezable hydration water is essential for the activation of protein dynamics. Decoupling of the dynamics between unfreezable and freezable hydration water could be the cause of the distinct contributions of hydration water to protein dynamics.
引用
收藏
页码:2172 / 2176
页数:5
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