

Title | CHARMM36m: an improved force field for folded and intrinsically disordered proteins. |
Publication Type | Journal Article |
Year of Publication | 2017 |
Authors | Huang, J, Rauscher, S, Nawrocki, G, Ran, T, Feig, M, de Groot, BL, Grubmüller, H, Mackerell, AD |
Journal | Nat Methods |
Volume | 14 |
Issue | 1 |
Pagination | 71-73 |
Date Published | 2017 Jan |
ISSN | 1548-7105 |
Keywords | Humans, 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. |
DOI | 10.1038/nmeth.4067 |
Alternate Journal | Nat. Methods |
PubMed ID | 27819658 |
PubMed Central ID | PMC5199616 |
Grant List | R01 GM072558 / GM / NIGMS NIH HHS / United States R01 GM084953 / GM / NIGMS NIH HHS / United States |