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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Topological and dynamical properties of Azurin anchored to a gold substrate as investigated by molecular dynamics simulation.
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Topological and dynamical properties of Azurin anchored to a gold substrate as investigated by molecular dynamics simulation.

机译：通过分子动力学模拟研究了固定在金基质上的天青素的拓扑和动力学性质。

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摘要

A classical molecular dynamics study of the electron transfer protein azurin, covalently bound to a gold substrate through its native disulphide group, is carried out at full hydration. With the aim of investigating the effects on the protein structure and dynamics as induced by the presence of an electric field, simulations are performed on neutral, positively and negatively charged substrates. A number of parameters, such as the average structure, the root mean square deviations and fluctuations, the intraprotein hydrogen bonds and solvent accessible surface of the protein, are monitored during 10 ns of run. The orientation, the height and the lateral size of the protein, with respect to the substrate are evaluated and compared with the experimental data obtained by scanning probe nanoscopies. The electron transfer properties between the copper redox center and the disulphide bridge bound to the substrate are investigated and briefly discussed.
机译：在完全水合的情况下，进行了电子转移蛋白天青蛋白的经典分子动力学研究，该蛋白通过其天然的二硫化物基团与金底物共价结合。为了研究电场的存在对蛋白质结构和动力学的影响，对中性，带正电和带负电的底物进行了模拟。在运行10 ns期间，监测许多参数，例如平均结构，均方根偏差和波动，蛋白质内氢键和蛋白质的溶剂可及表面。评估蛋白质相对于底物的方向，高度和横向尺寸，并将其与通过扫描探针纳米技术获得的实验数据进行比较。研究并简要讨论了铜氧化还原中心与结合到基材上的二硫桥之间的电子转移性质。

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