Structural characterization of an intrinsically disordered protein complex using integrated small-angle neutron scattering and computing.

ABSTRACT: Characterizing structural ensembles of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of proteins is essential for studying structure-function relationships. Due to the different neutron scattering lengths of hydrogen and deuterium, selective labeling and contrast matching in small-angle neutron scattering (SANS) becomes an effective tool to study dynamic structures of disordered systems. However, experimental timescales typically capture measurements averaged over multiple conformations, leaving complex SANS data for disentanglement. We hereby demonstrate an integrated method to elucidate the structural ensemble of a complex formed by two IDRs. We use data from both full contrast and contrast matching with residue-specific deuterium labeling SANS expe

SUBMITTER: Chen SH 

PROVIDER: S-EPMC10503416 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature