Novel Kinetic Intermediates Populated along the Folding Pathway of the Transmembrane β-Barrel OmpA.

ABSTRACT: We examined the folding of the β-barrel membrane protein OmpA from Escherichia coli. Although previous studies identified several intermediate states followed by a concerted translocation mechanism across the bilayer, some aspects of the pathway were still unclear, including the extent of secondary structure formation in the intermediate states and how the mechanism gave rise to multiple exponential phases in the folding kinetics. We addressed these questions by investigating the folding kinetics of the OmpA transmembrane β-barrel domain over a range of bilayer thicknesses, allowing us to observe different regions of the folding pathway. The fastest folding into the thinnest bilayers provided information about the later stages of the process, and the slowest folding into thicker bilayers r

SUBMITTER: Danoff EJ 

PROVIDER: S-EPMC5826654 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature