Combining THz spectroscopy and MD simulations to study protein-hydration coupling
Combining THz spectroscopy and MD simulations to study protein-hydration coupling
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DOI：
10.1016/j.ymeth.2010.05.007
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发表时间：
2010-09-01
期刊：
影响因子：
4.8
通讯作者：
Havenith, Martina
中科院分区：
文献类型：
--
作者：
Heyden, Matthias;Havenith, Martina
太赫兹光谱与MD模拟相结合，研究了蛋白质溶剂化壳中水的动力学性质。发现溶剂化动力学对几个水化层的长度尺度的影响明显大于对静态性质的影响。我们的实验表明，这种动态溶剂化壳的性质取决于蛋白质的折叠状态。动力学太赫兹吸收研究使我们能够观察到天然蛋白质折叠时动态溶剂化壳的形成。实验结果可以用MD模拟再现，这有助于从水动力学的延迟方面发展分子的理解。(C) 2010爱思唯尔公司版权所有。
THz spectroscopy is combined with MD simulations to study the dynamical properties of water in the solvation shell of proteins. The solvation dynamics is found to be influenced on length-scales of several hydration layers which is significantly more than what is found for static properties. Our experiments show that the properties of this dynamical solvation shell depend on the folding state of the protein. Kinetic THz absorption studies allow us to observe the formation of the dynamical solvation shell of the native protein upon folding. The experimental results can be reproduced using MD simulations which helps to develop a molecular understanding in terms of retardation of water dynamics. (C) 2010 Elsevier Inc. All rights reserved.