A genetically encoded anomalous SAXS ruler to probe the dimensions of intrinsically disordered proteins.

ABSTRACT: Intrinsically disordered proteins (IDPs) adopt ensembles of rapidly fluctuating heterogeneous conformations, influencing their binding capabilities and supramolecular transitions. The primary conformational descriptors for understanding IDP ensembles-the radius of gyration (R_G), measured by small-angle X-ray scattering (SAXS), and the root mean square (rms) end-to-end distance (R_E), probed by fluorescent resonance energy transfer (FRET)-are often reported to produce inconsistent results regarding IDP expansion as a function of denaturant concentration in the buffer. This ongoing debate surrounding the FRET-SAXS discrepancy raises questions about the overall reliability of either method for quantitatively studying IDP properties. To address this discrepan

SUBMITTER: Yu M 

PROVIDER: S-EPMC11648921 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature