Tournier Alexander L, Smith Jeremy C
Computational Molecular Biophysics, Interdisciplinary Center for Scientific Computing (IWR), Im Neuenheimer Feld 368, Universität Heidelberg, 69120 Heidelberg, Germany.
Phys Rev Lett. 2003 Nov 14;91(20):208106. doi: 10.1103/PhysRevLett.91.208106.
Proteins exhibit a solvent-driven dynamical transition at 180-220 K, manifested by nonlinearity in the temperature dependence of the average mean-square displacement. Here, molecular dynamics simulations of hydrated myoglobin show that the onset of the transition at approximately 180 K is characterized by the appearance of a single double-well principal component mode involving a global motion of two groups of helices. As the temperature is raised a few more quasiharmonic and multiminimum components successively appear. The results indicate an underlying simplicity in the protein dynamical transition.
蛋白质在180 - 220K时表现出溶剂驱动的动力学转变，这通过平均均方位移的温度依赖性中的非线性表现出来。在这里，水合肌红蛋白的分子动力学模拟表明，大约在180K时转变的开始特征是出现一个涉及两组螺旋整体运动的单一双阱主成分模式。随着温度进一步升高，相继出现一些准谐波和多阱成分。结果表明蛋白质动力学转变具有潜在的简单性。
