Atomistic characterization of collective protein-water-membrane dynamics.
Atomistic characterization of collective protein-water-membrane dynamics.
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DOI：
10.1039/c9cp00725c
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发表时间：
2019-07
期刊：
影响因子：
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通讯作者：
C. Päslack;Lars V. Schäfer;M. Heyden
中科院分区：
文献类型：
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作者：
C. Päslack;Lars V. Schäfer;M. Heyden
利用分子动力学模拟，研究了亚皮秒时间尺度上的相关振动运动和蛋白质-膜环境中的相关集体动力学。我们具体分析了相关的运动的膜相关蛋白质和脂质双层不同的分离距离。相关振动在两个生物分子表面之间持续25埃的距离。这些相关性是由水分子的分离层介导的，其集体性质被蛋白质和脂质双层界面的同时存在所改变。
Correlated vibrational motion on the sub-picosecond timescale and associated collective dynamics in a protein-membrane environment are characterized using molecular dynamics simulations. We specifically analyze correlated motion of a membrane-associated protein and a lipid bilayer for distinct separation distances. Correlated vibrations persist up to distances of 25 Å between both biomolecular surfaces. These correlations are mediated by separating layers of water molecules, whose collective properties are altered by the simultaneous presence of protein and lipid bilayer interfaces.