Kneller G R, Smith J C
IBM France, Paris.
J Mol Biol. 1994 Sep 23;242(3):181-5. doi: 10.1006/jmbi.1994.1570.
At temperatures above approximately 200 K the motions of atoms in globular proteins contain a non-vibrational component that gives rise to characteristic elastic and quasi-elastic neutron scattering profiles. There is evidence that the non-vibrational dynamics is required for protein function. Here we show by analysing a molecular dynamics simulation of myoglobin that the neutron scattering results from liquid-like rigid-body motion of the protein side-chains.
在温度高于约200 K时，球状蛋白质中原子的运动包含一个非振动成分，该成分会产生特征性的弹性和准弹性中子散射谱。有证据表明，非振动动力学对于蛋白质功能是必需的。在此，我们通过分析肌红蛋白的分子动力学模拟表明，中子散射源自蛋白质侧链的类液体刚体运动。
