One β hairpin after the other: Exploring mechanical unfolding pathways of the transmembrane β-barrel protein ompg

Research output: Contribution to journal › Research article › Contributed › peer-review

Contributors

  • K. Tanuj Sapra - , TUD Dresden University of Technology (Author)
  • Mehdi Damaghi - , TUD Dresden University of Technology (Author)
  • Stefan Köster - , TUD Dresden University of Technology (Author)
  • Özkan Yildiz - , TUD Dresden University of Technology (Author)
  • Werner Kühlbrandt - , TUD Dresden University of Technology (Author)
  • Daniel J. Müller - , Chair of Cellular Machines (Author)

Abstract

Roll out the barrel: By using singlemolecule force spectroscopy, a ß-barrelforming outer-membrane protein is unfolded for the first time. OmpC from E coli shows a surprising unfolding behavior: Singleβ, strands do not unfold individually but as β hairpins. These ß hairpins unfold one after another until the entire β-barrel membrane protein is unfolded (see structural representation).

Details

Original languageEnglish
Pages (from-to)8306-8308
Number of pages3
JournalAngewandte Chemie - International Edition
Volume48
Issue number44
Publication statusPublished - 19 Oct 2009
Peer-reviewedYes

External IDs

PubMed 19787673

Keywords

ASJC Scopus subject areas

Keywords

  • Barrel structures, Mechanical unfolding, Membrane proteins, Molecular interactions, Protein unfolding