Ontology highlight
ABSTRACT:
SUBMITTER: Schiffrin B
PROVIDER: S-EPMC5018216 | biostudies-literature | 2016 Sep
REPOSITORIES: biostudies-literature
Schiffrin Bob B Calabrese Antonio N AN Devine Paul W A PWA Harris Sarah A SA Ashcroft Alison E AE Brockwell David J DJ Radford Sheena E SE
Nature structural & molecular biology 20160725 9
The trimeric chaperone Skp sequesters outer-membrane proteins (OMPs) within a hydrophobic cage, thereby preventing their aggregation during transport across the periplasm in Gram-negative bacteria. Here, we studied the interaction between Escherichia coli Skp and five OMPs of varying size. Investigations of the kinetics of OMP folding revealed that higher Skp/OMP ratios are required to prevent the folding of 16-stranded OMPs compared with their 8-stranded counterparts. Ion mobility spectrometry- ...[more]