LARGE-AMPLITUDE NONLINEAR MOTIONS IN PROTEINS
LARGE-AMPLITUDE NONLINEAR MOTIONS IN PROTEINS
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DOI：
10.1103/physrevlett.68.2696
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发表时间：
1992-04-27
影响因子：
8.6
通讯作者：
GARCIA, AE
中科院分区：
文献类型：
--
作者：
GARCIA, AE
一个水合蛋白质，crambin的分子动力学计算表明，（i）相邻的二面角相关的蛋白质骨架中的局部过渡，和（ii）集体激发的幅度，代表相关的全球运动的蛋白质，样品多中心分布。多中心二面角和集体激发的时间依赖性显示从一个分布的中心到另一个分布的快速过渡，随后一段时间内围绕一个中心的阻尼，低振幅运动。整体非线性集体激发是分子中原子涨落的主要原因。适合于多模态构象的分析报告。
A molecular-dynamics calculation on a hydrated protein, crambin, demonstrates that (i) neighboring dihedral angles are correlated to local transitions in the protein backbone, and that (ii) the amplitude of collective excitations, representing correlated global motions in the protein, samples multicentered distributions. The time dependence of the multicentered dihedral and collective excitations show rapid transitions from the center of one distribution to another, followed for some time by damped, low-amplitude motions around one center. The global nonlinear collective excitations are responsible for most of the atomic fluctuations of the molecule. An analysis appropriate to multimodal conformations is reported.