Development of a polarizable force field for proteins via ab initio quantum chemistry: first generation model and gas phase tests.

ABSTRACT: We present results of developing a methodology suitable for producing molecular mechanics force fields with explicit treatment of electrostatic polarization for proteins and other molecular system of biological interest. The technique allows simulation of realistic-size systems. Employing high-level ab initio data as a target for fitting allows us to avoid the problem of the lack of detailed experimental data. Using the fast and reliable quantum mechanical methods supplies robust fitting data for the resulting parameter sets. As a result, gas-phase many-body effects for dipeptides are captured within the average RMSD of 0.22 kcal/mol from their ab initio values, and conformational energies for the di- and tetrapeptides are reproduced within the average RMSD of 0.43 kcal/mol from their quan

SUBMITTER: Kaminski GA 

PROVIDER: S-EPMC3963406 | biostudies-literature | 2002 Dec

REPOSITORIES: biostudies-literature