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

Jing Huang; Sarah Rauscher; Grzegorz Nawrocki; Ting Ran; Michael Feig; Bert L de Groot; Helmut Grubmüller; Alexander D MacKerell Jr

doi:10.1038/nmeth.4067

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

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

Authors

Jing Huang¹, Sarah Rauscher², Grzegorz Nawrocki³, Ting Ran¹, Michael Feig³, Bert L de Groot², Helmut Grubmüller², Alexander D MacKerell Jr¹

Affiliations

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural

MeSH terms

Humans
Hydrogen Bonding
Hydrophobic and Hydrophilic Interactions
Intrinsically Disordered Proteins / chemistry*
Molecular Dynamics Simulation*
Protein Conformation
Protein Folding*

Substances

Intrinsically Disordered Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding