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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Veröffentlicht in:	Nature methods 2017-01, Vol.14 (1), p.71-73
Hauptverfasser:	Huang, Jing, Rauscher, Sarah, Nawrocki, Grzegorz, Ran, Ting, Feig, Michael, de Groot, Bert L, Grubmüller, Helmut, MacKerell, Alexander D
Format:	Artikel
Sprache:	eng
Schlagworte:	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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Beschreibung
Zusammenfassung:	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.
ISSN:	1548-7091 1548-7105
DOI:	10.1038/nmeth.4067