title: Current status of protein force fields for molecular dynamics simulations.
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.
authors.affiliation: Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, 20 Penn Street HSFII, Baltimore, MD, 21201, USA.
authors.forename: Pedro E M
authors.initials: PE
authors.lastname: Lopes
authors.forename: Olgun
authors.initials: O
authors.lastname: Guvench
authors.forename: Alexander D
authors.initials: AD
authors.lastname: MacKerell
mesh_terms: D019731:Carbon-Nitrogen Ligases / Q000737:chemistry; D056004:Molecular Dynamics Simulation; D009113:Muramidase / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012984:Software; D013816:Thermodynamics
chemical_list: D010455:Peptides; D011506:Proteins; D009113:Muramidase; D019731:Carbon-Nitrogen Ligases; C020024:dethiobiotin synthetase