Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements.

ABSTRACT: Unfolded states of proteins and native states of intrinsically disordered proteins (IDPs) populate heterogeneous conformational ensembles in solution. The average sizes of these heterogeneous systems, quantified by the radius of gyration (R_G ), can be measured by small-angle X-ray scattering (SAXS). Another parameter, the mean dye-to-dye distance (R_E ) for proteins with fluorescently labeled termini, can be estimated using single-molecule Förster resonance energy transfer (smFRET). A number of studies have reported inconsistencies in inferences drawn from the two sets of measurements for the dimensions of unfolded proteins and IDPs in the absence of chemical denaturants. These differences are typically attributed to the influence of fluores

SUBMITTER: Fuertes G 

PROVIDER: S-EPMC5547626 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature