Comparative molecular dynamics simulations study of crystal environment effect on protein structure
Comparative molecular dynamics simulations study of crystal environment effect on protein structure
复制标题
晶体环境对蛋白质结构影响的比较分子动力学模拟研究
DOI：
10.1021/jp2125558
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
A.Kidera
中科院分区：
文献类型：
--
作者：
T.Terada;A.Kidera
Crystal structures of proteins are under the influence from the crystal environment. In this study, we used molecular dynamics (MD) simulations to explore the possibility of eliminating the effect of the crystal packing and recovering the structure in solution. Ten representative proteins were chosen from the Protein Structural Change Database as the target systems, and 50 ns MD stimulations starting from two crystal structures having different domain arrangements were performed for each. The MD trajectories of the relaxation processes upon the release from the crystal environment revealed that the behaviors of the proteins were classified into three groups: “single domain linker”, “harmonic motion”, and “large barrier”. We discuss the structural features common to the proteins in each group.
