CHARMM36m: an improved force field for folded and intrinsically disordered proteins.
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.
Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland, USA.
Jing
J
Huang
Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Sarah
S
Rauscher
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan, USA.
Grzegorz
G
Nawrocki
Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland, USA.
Ting
T
Ran
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan, USA.
Michael
0000-0001-9380-6422
M
Feig
Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Bert L
BL
de Groot
Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Helmut
H
Grubmüller
Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland, USA.
Alexander D
0000-0003-4290-182X
AD
MacKerell
D006801:Humans; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation; D017510:Protein Folding
D064267:Intrinsically Disordered Proteins