摘要
通过对猪囊尾蚴半胱氨酸蛋白酶Ts CL-1的结构模型进行分子动力学模拟,并对其进行模拟过程中的结构稳定性和动态结构柔性分析。结果表明,模拟过程中Ts CL-1总体结构相对稳定;分子的结构骨架具有较小的波动,而分子的表面环区和底物结合区域则具有较大的波动和较强的构象柔性。研究结果将为进一步深入研究Ts CL-1的动力学行为和功能关系奠定基础。
Using the Molecular Dynamics Simulation method, the dynamic structural stability and conformational flexibility of cysteine protease Ts CL-1 from Cysticercus cellulose have been investigated. The results indicate that Ts CL-1 contains an overall structural stability during the simulation. The results also indicate that the structural core of Ts CL-1 shows a small fluctuation amplitude, whereas most of the surface-exposed loops and the substrate binding sites experience significant conformational fluctuations and exhibit a highly structural flexibility. The results of this article will provide a solid basis for further studying the relationship between dynamic structural features and functions of Ts CL-1.
出处
《大理大学学报》
CAS
2017年第6期55-58,共4页
Journal of Dali University
基金
大学生科研基金资助项目(KYSX201615)
关键词
半胱氨酸蛋白酶TsCL-1
分子动力学模拟
动态结构柔性
结构功能研究
Cysteine protease TsCL-1
molecular dynamics simu-lations
dynamic structural flexibility
structure and function relationship