Structural Characterization of N-WASP Domain V Using MD Simulations with NMR and SAXS Data.

ABSTRACT: Because of their large conformational heterogeneity, structural characterization of intrinsically disordered proteins (IDPs) is very challenging using classical experimental methods alone. In this study, we use NMR and small-angle x-ray scattering (SAXS) data with multiple molecular dynamics (MD) simulations to describe the conformational ensemble of the fully disordered verprolin homology domain of the neural Aldrich syndrome protein involved in the regulation of actin polymerization. First, we studied several back-calculation software of SAXS scattering intensity and optimized the adjustable parameters to accurately calculate the SAXS intensity from an atomic structure. We also identified the most appropriate force fields for MD simulations of this IDP. Then, we analyzed four conformatio

SUBMITTER: Chan-Yao-Chong M 

PROVIDER: S-EPMC6451034 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature