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. 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

Jing Huang  1 , Sarah Rauscher  2 , Grzegorz Nawrocki  3 , Ting Ran  1 , Michael Feig  3 , Bert L de Groot  2 , Helmut Grubmüller  2 , Alexander D MacKerell Jr  1
Affiliations

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

Jing Huang et al. Nat Methods. 2017 Jan.

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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Figures

Figure 1
Figure 1
SAXS profiles of the RS peptide. Ensemble-averaged scattering curves from the C36 simulation (blue) and the C36m simulation (red) are plotted, with the experimental curve shown with error in gray. The nonweighted error function χ2 as defined in Ref. was 0.63 using C36, and 0.12 using C36m. The error bars represent the standard deviation computed by dividing the conformational ensembles in two, and computing the average SAXS profile for each half separately. For the C36m ensemble, the error bars are smaller than the line width.
See this image and copyright information in PMC

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