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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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Metadata

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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CoChat. (2026). Citation check: CHARMM36m: an improved force field for folded and intrinsically disordered proteins. https://app.cochat.ai/papers/10.1038/nmeth.4067
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Huang, J., Rauscher, S., Nawrocki, G., Ran, T., Feig, M., de Groot, B. L., Grubmüller, H., & MacKerell, A. D. (2017). CHARMM36m: an improved force field for folded and intrinsically disordered proteins. Nature Methods. https://doi.org/10.1038/nmeth.4067

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