CHARMM36m: An improved force field for folded and intrinsically disordered proteins

被引：0
|
作者：
Huang J. [1 ]
Rauscher S. [2 ]
Nawrocki G. [3 ]
Ran T. [1 ]
Feig M. [3 ]
De Groot B.L. [2 ]
Grubmüller H. [2 ]
MacKerell A.D., Jr. [1 ]
机构：
[1] Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD
[2] Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Göttingen
[3] Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI
来源：
Nature Methods | 2017年 / 14卷 / 1期
基金：
美国国家卫生研究院;
关键词：
D O I：
10.1038/nmeth.4067
中图分类号：
学科分类号：
摘要：
The all-atom additive CHARMM36 protein force field is widely used in molecular modeling and simulations. We present its refinement, CHARMM36m (http://mackerell.umaryland.edu/charmm-ff.shtml), with improved accuracy in generating polypeptide backbone conformational ensembles for intrinsically disordered peptides and proteins. © 2017 Nature America, Inc., part of Springer Nature. All rights reserved.
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收藏
页码：71 / 73
页数：2
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