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, Grubm├╝ller, 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