Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
J Chem Phys. 2013 Mar 7;138(9):094112. doi: 10.1063/1.4793625.
In order to characterise the dynamics of proteins, a well-established method is to incorporate experimental parameters as replica-averaged structural restraints into molecular dynamics simulations. Here, we justify this approach in the case of interproton distance information provided by nuclear Overhauser effects by showing that it generates ensembles of conformations according to the maximum entropy principle. These results indicate that the use of replica-averaged structural restraints in molecular dynamics simulations, given a force field and a set of experimental data, can provide an accurate approximation of the unknown Boltzmann distribution of a system.
为了描述蛋白质的动力学特性，可以采用一种成熟的方法，即将实验参数作为复制平均结构约束纳入分子动力学模拟中。在这里，我们通过证明该方法可以根据最大熵原理生成构象系综，从而证明了核 Overhauser 效应提供的质子间距离信息的这种方法是合理的。这些结果表明，在给定力场和一组实验数据的情况下，在分子动力学模拟中使用复制平均结构约束可以提供对系统未知 Boltzmann 分布的准确近似。
