Hinsen Konrad, Kneller Gerald R
Centre de Biophysique Moléculaire, CNRS UPR 4301, Rue Charles Sadron, 45071 Orléans Cedex 2, France.
Proteins. 2008 Mar;70(4):1235-42. doi: 10.1002/prot.21655.
The influence of solvent on the slow internal dynamics of proteins is studied by comparing molecular dynamics simulations of solvated and unsolvated lysozyme. The dynamical trajectories are projected onto the protein's normal modes in order to obtain a separate analysis for each of the associated time scales. The results show that solvent effects are important for the slowest motions (below approximately 1 ps(-1)) but negligible for faster motions. The damping effects seen in the latter show that the principal source of friction in protein dynamics is not the solvent, but the protein itself.
通过比较溶剂化和非溶剂化溶菌酶的分子动力学模拟，研究了溶剂对蛋白质缓慢内部动力学的影响。将动力学轨迹投影到蛋白质的正常模式上，以便对每个相关的时间尺度进行单独分析。结果表明，溶剂效应对于最慢的运动（低于约1 ps⁻¹）很重要，但对于较快的运动可忽略不计。后者中看到的阻尼效应表明，蛋白质动力学中摩擦的主要来源不是溶剂，而是蛋白质本身。
