University of Tennessee/Oak Ridge National Laboratory Center for Molecular Biophysics, P.O.Box 2008, Oak Ridge Tennessee 37831-6164, USA.
Phys Rev Lett. 2011 Sep 30;107(14):148102. doi: 10.1103/PhysRevLett.107.148102.
A simplified description of the 295 K dynamics of a globular protein over a wide frequency range (1-1000 GHz) is obtained by combining neutron scattering of lysozyme with molecular dynamics simulation. The molecular dynamics simulation agrees quantitatively with experiment for both the protein and the hydration water and shows that, whereas the hydration water molecules subdiffuse, the protein atoms undergo confined motion decomposable into three distinct classes: localized diffusion, methyl group rotations, and jumps. Each of the three classes gives rise to a characteristic neutron susceptibility signal.
通过将溶菌酶的中子散射与分子动力学模拟相结合，获得了在较宽频率范围内（1-1000GHz）球形蛋白质的 295K 动力学的简化描述。分子动力学模拟对蛋白质和水合水分子都进行了定量的实验验证，表明虽然水合水分子亚扩散，但蛋白质原子经历了可分解为三个不同类别：局部扩散、甲基旋转和跳跃的受限运动。每一类都会产生一个特征的中子磁化率信号。
