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

MPS-Authors
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Rauscher,  S.
Department of Theoretical and Computational Biophysics, MPI for Biophysical Chemistry, Max Planck Society;

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de Groot,  B. L.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Grubmüller,  H.
Department of Theoretical and Computational Biophysics, MPI for Biophysical Chemistry, Max Planck Society;

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Fulltext (public)

2367828.pdf
(Publisher version), 382KB

Supplementary Material (public)

2367828_Suppl.pdf
(Supplementary material), 5MB

Citation

Huang, J., Rauscher, S., Nawrocki, G., Ran, T., Feig, M., de Groot, B. L., et al. (2017). CHARMM36m: An improved force field for folded and intrinsically disordered proteins. Nature Methods, 14(1), 71-73. doi:10.1038/nmeth.4067.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-11D6-A
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.