High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape.

ABSTRACT: A complete description of the pathways and mechanisms of protein folding requires a detailed structural and energetic characterization of the conformational ensemble along the entire folding reaction coordinate. Simulations can provide this level of insight for small proteins. In contrast, with the exception of hydrogen exchange, which does not monitor folding directly, experimental studies of protein folding have not yielded such structural and energetic detail. NMR can provide residue specific atomic level structural information, but its implementation in protein folding studies using chemical or temperature perturbation is problematic. Here we present a highly detailed structural and energetic map of the entire folding landscape of the leucine-rich repeat protein, pp32 (Anp32), obtained

SUBMITTER: Fossat MJ 

PROVIDER: S-EPMC5153537 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature