Coupling between lysozyme and trehalose dynamics: Microscopic insights from molecular-dynamics simulations
Coupling between lysozyme and trehalose dynamics: Microscopic insights from molecular-dynamics simulations
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DOI：
10.1063/1.2159471
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发表时间：
2006-01-21
影响因子：
4.4
通讯作者：
Sokolov, AP
中科院分区：
文献类型：
--
作者：
Dirama, TE;Curtis, JE;Sokolov, AP
我们已经进行了分子动力学模拟完全灵活的全原子模型的蛋白质溶菌酶浸泡在海藻糖，一种有效的生物防腐剂，探索它们之间的动力学耦合的性质和程度的目的。我们的研究表明，在很宽的温度范围内的强耦合。我们发现，非谐行为的发生是由海藻糖玻璃中的动力学和弛豫过程的变化决定的。蛋白质-海藻糖偶联的物理起源可追溯到蛋白质和溶剂之间界面处形成的氢键。此外，蛋白质-溶剂氢键被发现控制蛋白质的结构松弛。的蛋白质的动力学被发现是异质的，表面和核心原子的运动有不同的依赖于温度，此外，表面原子比核心原子的溶剂的动力学更敏感。从溶剂的角度来看，我们发现，蛋白质表面附近的动力学表现出意想不到的增强流动性相比，散装。这些结果揭示了蛋白质-溶剂系统动力学耦合的微观起源。(c)2006年，美国物理学会。
We have carried out molecular-dynamics simulations on fully flexible all-atom models of the protein lysozyme immersed in trehalose, an effective biopreservative, with the purpose of exploring the nature and extent of the dynamical coupling between them. Our study shows a strong coupling over a wide range of temperatures. We found that the onset of anharmonic behavior was dictated by changes in the dynamics and relaxation processes in the trehalose glass. The physical origin of protein-trehalose coupling was traced to the hydrogen bonds formed at the interface between the protein and the solvent. Moreover, protein-solvent hydrogen bonding was found to control the structural relaxation of the protein. The dynamics of the protein was found to be heterogeneous; the motions of surface and core atoms had different dependencies on temperature and, in addition, the surface atoms were more sensitive to the dynamics of the solvent than the core atoms. From the solvent perspective we found that the dynamics near the protein surface showed an unexpected enhanced mobility compared to the bulk. These results shed some light on the microscopic origins of the dynamical coupling in protein-solvent systems. (c) 2006 American Institute of Physics.