Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle

被引：157

作者：

Cavalli, Andrea ^{[1
,2
]}

Camilloni, Carlo ^{[1
]}

Vendruscolo, Michele ^{[1
]}

机构：

[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England

[2] Inst Res Biomed, CH-6500 Bellinzona, Switzerland

来源：

JOURNAL OF CHEMICAL PHYSICS | 2013年 / 138卷 / 09期

基金：

英国生物技术与生命科学研究理事会;

关键词：

ATOMIC-LEVEL CHARACTERIZATION; PROTEIN-STRUCTURE; CONFORMATIONAL DYNAMICS; STRUCTURE REFINEMENT; DISTANCE RESTRAINTS; INFORMATION-THEORY; ENERGY LANDSCAPES; NMR DATA; TIME; PEPTIDE;

D O I：

10.1063/1.4793625

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070305 [高分子化学与物理];

摘要：

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. (C) 2013 American Institute of Physics. [http://dx.doi.org/10.1063/1.4793625]

引用

页数：5

共 52 条

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[2]

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