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

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Huang, Jing, Rauscher, Sarah, Nawrocki, Grzegorz, Ran, Ting, Feig, Michael, de Groot, Bert L, Grubmüller, Helmut, MacKerell, Alexander D·2017·Nature Methods

DOI 10.1038/nmeth.4067

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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.

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Authors: Huang, J., Rauscher, S., Nawrocki, G., Ran, T., Feig, M., de Groot, B. L., Grubmüller, H., & MacKerell, A. D.
Venue: Nature Methods
Publisher: Springer Science and Business Media LLC
Published: 2016-11-07
Volume: 14
Issue: 1
Pages: 71-73
ISSN: 1548-7091 (ISSN-L)
1548-7105
DOI: 10.1038/nmeth.4067
OpenAlex: W2555870966
Cited by: 7,285
References: 0
FWCI: 78.25
Type: journal article
Language: en
Open access: bronze
Licence: www.springer.com/tdm (tdm)

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

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