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

  • Mehdi Damaghi
  • , Stefan Köster
  • , Christian A. Bippes
  • , Özkan Yildiz
  • , Daniel J. Müller
  • Max Planck Institute of Biophysics
  • Swiss Federal Institute of Technology Zurich

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

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.

Original languageEnglish
Pages (from-to)7422-7424
Number of pages3
JournalAngewandte Chemie - International Edition
Volume50
Issue number32
DOIs
StatePublished - Aug 1 2011

Keywords

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

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