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Nat Methods. 2017 Jan;14(1):71-73. doi: 10.1038/nmeth.4067. Epub 2016 Nov 7.

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

Author information

1
Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland, USA.
2
Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
3
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan, USA.

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.

PMID:
27819658
PMCID:
PMC5199616
DOI:
10.1038/nmeth.4067
[Indexed for MEDLINE]
Free PMC Article

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