M
Michael Feig
Researcher at Michigan State University
Publications - 193
Citations - 28987
Michael Feig is an academic researcher from Michigan State University. The author has contributed to research in topics: Molecular dynamics & Solvation. The author has an hindex of 54, co-authored 181 publications receiving 24201 citations. Previous affiliations of Michael Feig include Scripps Research Institute & RIKEN Quantitative Biology Center.
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Journal ArticleDOI
CHARMM: the biomolecular simulation program.
Bernard R. Brooks,Charles L. Brooks,Alexander D. MacKerell,Lennart Nilsson,Robert J. Petrella,Benoît Roux,Youngdo Won,Georgios Archontis,Christian Bartels,Stefan Boresch,Amedeo Caflisch,Leo S. D. Caves,Qiang Cui,Aaron R. Dinner,Michael Feig,Stefan Fischer,Jiali Gao,Milan Hodošček,Wonpil Im,K. Kuczera,Themis Lazaridis,Jianpeng Ma,V. Ovchinnikov,Emanuele Paci,Richard W. Pastor,Carol Beth Post,Jingzhi Pu,M. Schaefer,Bruce Tidor,Richard M. Venable,H. L. Woodcock,Xiongwu Wu,Wei Yang,Darrin M. York,Martin Karplus,Martin Karplus +35 more
TL;DR: An overview of the CHARMM program as it exists today is provided with an emphasis on developments since the publication of the original CHARMM article in 1983.
Journal ArticleDOI
Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone φ, ψ and side-chain χ(1) and χ(2) dihedral angles.
Robert B. Best,Xiao Zhu,Jihyun Shim,Pedro E. M. Lopes,Jeetain Mittal,Michael Feig,Alexander D. MacKerell +6 more
TL;DR: The results indicate that the revised CHARMM 36 parameters represent an improved model for the modeling and simulation studies of proteins, including studies of protein folding, assembly and functionally relevant conformational changes.
Journal ArticleDOI
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 +7 more
TL;DR: The all-atom additive CHARMM36 protein force field is refinement is presented, with improved accuracy in generating polypeptide backbone conformational ensembles for intrinsically disordered peptides and proteins.
Journal ArticleDOI
Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations.
TL;DR: To improve the treatment of the peptide backbone, quantum mechanical and molecular mechanical calculations were undertaken on the alanine, glycine, and proline dipeptides, and the results were combined with molecular dynamics simulations of proteins in crystal and aqueous environments to enhance the quality of the CHARMM force field.
Journal ArticleDOI
Improved treatment of the protein backbone in empirical force fields.
TL;DR: Inclusion of this correction with the CHARMM22 all-atom protein force field is shown to lead to significant improvement in the treatment of the conformational energies of both the peptide model compound, the alanine dipeptide, and of proteins in their crystal environment.