Current status of protein force fields for molecular dynamics simulations.

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TitleCurrent status of protein force fields for molecular dynamics simulations.
Publication TypeJournal Article
Year of Publication2015
AuthorsLopes, PEM, Guvench, O, Mackerell, AD
JournalMethods Mol Biol
Volume1215
Pagination47-71
Date Published2015
ISSN1940-6029
KeywordsCarbon-Nitrogen Ligases, Molecular Dynamics Simulation, Muramidase, Peptides, Proteins, Software, Thermodynamics
Abstract

The current status of classical force fields for proteins is reviewed. These include additive force fields as well as the latest developments in the Drude and AMOEBA polarizable force fields. Parametrization strategies developed specifically for the Drude force field are described and compared with the additive CHARMM36 force field. Results from molecular simulations of proteins and small peptides are summarized to illustrate the performance of the Drude and AMOEBA force fields.

DOI10.1007/978-1-4939-1465-4_3
Alternate JournalMethods Mol. Biol.
PubMed ID25330958
PubMed Central IDPMC4554537
Grant ListR01 GM072558 / GM / NIGMS NIH HHS / United States
R15 GM099022 / GM / NIGMS NIH HHS / United States
GM072558 / GM / NIGMS NIH HHS / United States