Simulations of intrinsically disordered proteins require accurate force fields. Two issues are critical for accurate protein force field development: (1) How to obtain intrinsic conformational potentials of each amino acid; (2) How to effectively incorporate these potentials into a force field. We have developed novel strategies to derive intrinsic conformational potentials by statistical analysis of protein coil library. These conformational features have been used to develop residue-specific force fields RSFF1 and RSFF2 by modifying OPLS-AA and Amber-99sb force fields, respectively, using residue-specific parameters. These force fields have been shown to reproduce 3JHNHa-coupling constants of a series of peptides very well, to fold a series of proteins, and to refine a series of protein structures. They also have advantageous in the studies of intrinsically disordered proteins and cyclic peptides.

Residue-specific protein force fields RSFF1 and RSFF2

254th National Meeting (2017)

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