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

An all-atom protein force field, CHARMM36m, offers improved accuracy for simulating intrinsically disordered peptides and proteins. The all-atom additive CHARMM36 protein force field is widely used in molecular modeling and simulations. We present its refinement, CHARMM36m ( http://mackerell.umaryla...

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Published inNature methods Vol. 14; no. 1; pp. 71 - 73
Main Authors Huang, Jing, Rauscher, Sarah, Nawrocki, Grzegorz, Ran, Ting, Feig, Michael, de Groot, Bert L, Grubmüller, Helmut, MacKerell, Alexander D
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 01.01.2017
Nature Publishing Group
Subjects
631/114/2411
631/114/794
631/1647/2258
631/45/612
631/57/2266
82
Analysis
Bioinformatics
Biological Microscopy
Biological Techniques
Biomedical and Life Sciences
Biomedical Engineering/Biotechnology
brief-communication
Eukaryotes
Humans
Hydrogen Bonding
Hydrophobic and Hydrophilic Interactions
Intrinsically Disordered Proteins - chemistry
Life Sciences
Molecular Dynamics Simulation
Molecular modeling
Peptides
Polypeptides
Protein binding
Protein Conformation
Protein Folding
Proteins
Proteomics
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Summary:An all-atom protein force field, CHARMM36m, offers improved accuracy for simulating intrinsically disordered peptides and proteins. 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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:1548-7091
1548-7105
DOI:10.1038/nmeth.4067