A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering.

ABSTRACT: Natively unfolded proteins play key roles in normal and pathological biochemical processes. Despite their importance for function, this category of proteins remains beyond the reach of classical structural biology because of their inherent conformational heterogeneity. We present a description of the intrinsic conformational sampling of unfolded proteins based on residue-specific /Psi propensities from loop regions of a folded protein database and simple volume exclusion. This approach is used to propose a structural model of the 57-aa, natively disordered region of the nucleocapsid-binding domain of Sendai virus phosphoprotein. Structural ensembles obeying these simple rules of conformational sampling are used to simulate averaged residual dipolar couplings (RDCs) and small-angle x-ray sc

SUBMITTER: Bernado P 

PROVIDER: S-EPMC1287987 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature