Impact of electronic polarizability on protein-functional group interactions.

ABSTRACT: Interactions of proteins with functional groups are key to their biological functions, making it essential that they be accurately modeled. To investigate the impact of the inclusion of explicit treatment of electronic polarizability in force fields on protein-functional group interactions, the additive CHARMM and Drude polarizable force field are compared in the context of the Site-Identification by Ligand Competitive Saturation (SILCS) simulation methodology from which functional group interaction patterns with five proteins for which experimental binding affinities of multiple ligands are available, were obtained. The explicit treatment of polarizability produces significant differences in the functional group interactions in the ligand binding sites including overall enhanced binding o

SUBMITTER: Goel H 

PROVIDER: S-EPMC7194236 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature