Bizzarri Anna Rita
Biophysics and Nanoscience Centre, CNISM, Dipartimento di Scienze Ambientali, Università della Tuscia, I-01100 Viterbo, Italy.
Biophys Chem. 2006 Aug 1;122(3):206-14. doi: 10.1016/j.bpc.2006.03.012. Epub 2006 Mar 28.
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.
对通过其天然二硫基团与金基底共价结合的电子转移蛋白天青蛋白进行了完全水合状态下的经典分子动力学研究。为了研究电场存在对蛋白质结构和动力学的影响，在中性、带正电和带负电的基底上进行了模拟。在10纳秒的运行过程中监测了许多参数，如平均结构、均方根偏差和波动、蛋白质内氢键以及蛋白质的溶剂可及表面积。评估了蛋白质相对于基底的取向、高度和横向尺寸，并与通过扫描探针纳米显微镜获得的实验数据进行了比较。研究并简要讨论了铜氧化还原中心与结合在基底上的二硫桥之间的电子转移性质。
