Local and non-local topological information in the denatured state ensemble of a β-barrel protein.

ABSTRACT: The folding of predominantly β-sheet proteins is complicated by the presence of a large number of non-local interactions in their native states, which increase the ruggedness of their folding energy landscapes. However, forming non-local contacts early in folding or even in the unfolded state can smooth the energy landscape and facilitate productive folding. We report that several sequence regions of a β-barrel protein, cellular retinoic acid-binding protein 1 (CRABP1), populate native-like secondary structure to a significant extent in the denatured state in 8 M urea. In addition, we provide evidence for both local and non-local interactions in the denatured state of CRABP1. NMR chemical shift perturbations (CSPs) under denaturing conditions upon substitution of single residues by mutatio

SUBMITTER: Thakur AK 

PROVIDER: S-EPMC6237703 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature