Centre de Biophysique Moléculaire, CNRS and Université d'Orléans, Rue Charles Sadron, 45071 Orléans, France.
Institut Laue Langevin, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France.
J Chem Phys. 2019 Apr 28;150(16):161104. doi: 10.1063/1.5094625.
In this paper, we show that subtle changes in the internal dynamics of human acetylcholinesterase upon ligand binding can be extracted from quasielastic neutron scattering data by employing a nonexponential relaxation model for the intermediate scattering function. The relaxation is here described by a stretched Mittag-Leffler function, which exhibits slow power law decay for long times. Our analysis reveals that binding of a Huperzine A ligand increases the atomic motional amplitudes of the enzyme and slightly slows down its internal diffusive motions. This result is interpreted within an energy landscape picture for the motion of the hydrogen atoms.
在本文中，我们通过对中间散射函数采用非指数弛豫模型，从准弹性中子散射数据中提取出配体结合后人类乙酰胆碱酯酶内部动力学的细微变化。这里的弛豫由拉伸的 Mittag-Leffler 函数描述，该函数在长时间内呈现出缓慢的幂律衰减。我们的分析表明，Huperzine A 配体的结合增加了酶的原子运动幅度，并稍微减缓了其内部扩散运动。这一结果在氢原子运动的能量景观图中得到了解释。
