Maximum Entropy Optimized Force Field for Intrinsically Disordered Proteins.

ABSTRACT: Intrinsically disordered proteins (IDPs) constitute a significant fraction of eukaryotic proteomes. High-resolution characterization of IDP conformational ensembles can help elucidate their roles in a wide range of biological processes but remains challenging both experimentally and computationally. Here, we present a generic algorithm to improve the accuracy of coarse-grained IDP models using a diverse set of experimental measurements. It combines maximum entropy optimization and least-squares regression to systematically adjust model parameters and improve the agreement between simulation and experiment. We successfully applied the algorithm to derive a transferable force field, which we term the maximum entropy optimized force field (MOFF), for de novo prediction of IDP structures. Stat

SUBMITTER: Latham AP 

PROVIDER: S-EPMC7241281 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature