Roh J H, Novikov V N, Gregory R B, Curtis J E, Chowdhuri Z, Sokolov A P
Department of Polymer Science, The University of Akron, Akron, OH 44325-3909, USA.
Phys Rev Lett. 2005 Jul 15;95(3):038101. doi: 10.1103/PhysRevLett.95.038101. Epub 2005 Jul 12.
Two onsets of anharmonicity are observed in the dynamics of the protein lysozyme. One at T approximately 100 K appears in all samples regardless of hydration level and is consistent with methyl group rotation. The second, the well-known dynamical transition at T approximately 200-230 K, is only observed at a hydration level h greater than approximately 0.2 and is ascribed to the activation of an additional relaxation process. Its variation with hydration correlates well with variations of catalytic activity suggesting that the relaxation process is directly related to the activation of modes required for protein function.
在溶菌酶的动力学过程中观察到了两种非谐性起始现象。一种出现在约100 K的温度下，在所有样品中都能观察到，与甲基旋转有关，且与水合水平无关。第二种是在约200 - 230 K温度下的著名动力学转变，仅在水合水平h大于约0.2时观察到，这归因于额外弛豫过程的激活。其随水合作用的变化与催化活性的变化密切相关，这表明弛豫过程与蛋白质功能所需模式的激活直接相关。
