Refining All-Atom Protein Force Fields for Polar-Rich, Prion-like, Low-Complexity Intrinsically Disordered Proteins.

ABSTRACT: Significant efforts in the past decade have given us highly accurate all-atom protein force fields for molecular dynamics (MD) simulations of folded and disordered proteins. These simulations, complemented with experimental data, provide new insights into molecular interactions that underlie the physical properties of proteins, especially for intrinsically disordered proteins (IDPs) for which defining the heterogeneous structural ensemble is hugely challenging by experiments alone. Consequently, the accuracy of these protein force fields is of utmost importance to ensure reliable simulated conformational data. Here, we first assess the accuracy of current state-of-the-art force fields for IDPs (ff99SBws and ff03ws) applied to disordered proteins of low amino acid sequence complexity that c

SUBMITTER: Tang WS 

PROVIDER: S-EPMC7880584 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature