A self-consistent description of the conformational behavior of chemically denatured proteins from NMR and small angle scattering.

ABSTRACT: Characterization of the conformational properties of unfolded proteins is essential for understanding the mechanisms of protein folding and misfolding. This information is also fundamental to determining the relationship between flexibility and function in the highly diverse families of intrinsically disordered proteins. Here we present a self-consistent model of conformational sampling of chemically denatured proteins in agreement with experimental data reporting on long-range distance distributions in unfolded proteins using small-angle x-ray scattering and nuclear magnetic resonance pulse-field gradient-based measurements. We find that standard statistical coil models, selected from folded protein databases with secondary structural elements removed, need to be refined to correct backbo

SUBMITTER: Bernado P 

PROVIDER: S-EPMC2776250 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature