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

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TitleCHARMM36m: an improved force field for folded and intrinsically disordered proteins.
Publication TypeJournal Article
Year of Publication2017
AuthorsHuang, J, Rauscher, S, Nawrocki, G, Ran, T, Feig, M, de Groot, BL, Grubmüller, H, Mackerell, AD
JournalNat Methods
Volume14
Issue1
Pagination71-73
Date Published2017 Jan
ISSN1548-7105
KeywordsHumans, Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Intrinsically Disordered Proteins, Molecular Dynamics Simulation, Protein Conformation, Protein Folding
Abstract

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.

DOI10.1038/nmeth.4067
Alternate JournalNat. Methods
PubMed ID27819658
PubMed Central IDPMC5199616
Grant ListR01 GM072558 / GM / NIGMS NIH HHS / United States
R01 GM084953 / GM / NIGMS NIH HHS / United States