An Extended Guinier Analysis for Intrinsically Disordered Proteins.

ABSTRACT: Guinier analysis allows model-free determination of the radius of gyration (R_g) of a biomolecule from X-ray or neutron scattering data, in the limit of very small scattering angles. Its range of validity is well understood for globular proteins, but is known to be more restricted for unfolded or intrinsically disordered proteins (IDPs). We have used ensembles of disordered structures from molecular dynamics simulations to investigate which structural properties cause deviations from the Guinier approximation at small scattering angles. We find that the deviation from the Guinier approximation is correlated with the polymer scaling exponent ν describing the unfolded ensemble. We therefore introduce an empirical, ν-dependent, higher-order correction term, to augment the standard G

SUBMITTER: Zheng W 

PROVIDER: S-EPMC6093220 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature