期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 22, 期 32, 页码 18132-18140出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0cp02416c
关键词
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资金
- NSF China [11974239, 31630002]
- Innovation Program of Shanghai Municipal Education Commission
- Shanghai Jiao Tong university Multidisciplinary research fund of medicine and engineering [YG 2016QN13]
The interaction between water and biomacromolecules is of fundamental interest in biophysics, biochemistry and physical chemistry. By combining neutron scattering and molecular dynamics simulations on a perdeuterated protein at a series of hydration levels, we demonstrated that the translational motion of water is slowed down more significantly than its rotation, when water molecules approach the protein molecule. Further analysis of the simulation trajectories reveals that the observed decoupling results from the fact that the translational motion of water is more correlated over space and more retarded by the charged/polar residues and spatial confinement on the protein surface, than the rotation. Moreover, around the stable protein residues (with smaller atomic fluctuations), water exhibits more decoupled dynamics, indicating a connection between the observed translation-rotation decoupling in hydration water and the local stability of the protein molecule.
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