One β hairpin follows the other: Exploring refolding pathways and kinetics of the transmembrane β-barrel protein OmpG

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Mehdi Damaghi - (Author)
  • Stefan Köster - (Author)
  • Christian A. Bippes - (Author)
  • Özkan Yildiz - (Author)
  • Daniel J. Müller - , Chair of Cellular Machines (Author)

Abstract

One by one: The β-barrel-forming outer-membrane protein G (OmpG) from E. coli can be folded into the native lipid membrane by using single-molecule force spectroscopy. Surprisingly, single β strands do not refold individually but as β hairpins that refold consecutively until the entire β-barrel membrane protein is refolded (see picture). This mechanism significantly advances the understanding of current folding models of β-barrel proteins.

Details

Original languageEnglish
Pages (from-to)7422-7424
Number of pages3
JournalAngewandte Chemie - International Edition
Volume50
Issue number32
Publication statusPublished - 1 Aug 2011
Peer-reviewedYes

External IDs

PubMed 21692155

Keywords

ASJC Scopus subject areas

Keywords

  • β hairpins, mechanical unfolding, membrane proteins, protein folding, single-molecule force spectroscopy