Barnase中氢键与热稳定性关系的动力学模拟研究  

Insight into Hydrogen Bond Thermal Stability Relationship of Barnase by Molecular Dynamics Simulation

作　　者：陈志国[1] 傅毅[1] 须文波[1] 

机构地区：[1]轻工过程先进控制教育部重点实验室,江南大学物联网工程学院,江苏无锡214122

出　　处：《生物技术》2013年第6期89-92,共4页Biotechnology

基　　金：中央高校基本科研业务费专项资金("无线传感器网络群机器人智能调度研究";JUSRP111A46)资助~~

摘　　要：目的：研究Bamase中分子内非共价键相互作用一氢键在热压力下如何发生变化，以及其对蛋白质热稳定性的影响。方法：采用NAMD软件对Barnase进行高温分子动力学模拟，VMD软件进行可视化分析。结果：随着模拟温度的升高，蛋白质内部氢键的数量减少约50％左右，占有时间也明显缩短；400K温度下，占有时间减少有15％-98％，多数减少约50％左右。蛋白质的稳定性与氢键的数量、氢键的占有率、形成氢键的氨基酸空间位置以及形成的氢键的空间位置都相关。结论：氢键的稳定存在对于蛋白质Barnase抵抗高温有着重要作用。Objective：This study is to investigate the contribution of non - covalent intramolecular interactions - hydrogen bond to protein stability and how changes in these interactions in response to thermal stress. Method：All simulations were performed using the molecular dynamics program NAMD. Visualization and data analysis were done with the program VMD. Result： The number of hydrogen bond de- creased about 50% when temperature increases. The occupied time of hydrogen bond descended to about 15% -98% at 400K. The Bar- nase protein stability is related to the number of hydrogen bond, occupancy time, amino acid position of the formation of hydrogen bond and the spatial position of hydrogen bond. Conclusion： These resuhs suggest hydrogen bond is an important factor in enhancing the thermal sta- bility of Barnase.

关 键 词：解淀粉芽孢杆菌核糖核酸酶 热稳定 氢键 分子动力学模拟 蛋白质设计 

分 类 号：TP391.9[自动化与计算机技术—计算机应用技术]