Investigating the Conformational Ensembles of Intrinsically Disordered Proteins with a Simple Physics-Based Model.

ABSTRACT: Intrinsically disordered proteins (IDPs) play an important role in an array of biological processes but present a number of fundamental challenges for computational modeling. Recently, simple polymer models have regained popularity for interpreting the experimental characterization of IDPs. Homopolymer theory provides a strong foundation for understanding generic features of phenomena ranging from single-chain conformational dynamics to the properties of entangled polymer melts, but is difficult to extend to the copolymer context. This challenge is magnified for proteins due to the variety of competing interactions and large deviations in side-chain properties. In this work, we apply a simple physics-based coarse-grained model for describing largely disordered conformational ensembles of p

SUBMITTER: Zhao Y 

PROVIDER: S-EPMC7246978 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature