These authors contributed equally to this work.
One β Hairpin after the Other: Exploring Mechanical Unfolding Pathways of the Transmembrane β-Barrel Protein OmpG†
Article first published online: 28 SEP 2009
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 48, Issue 44, pages 8306–8308, October 19, 2009
How to Cite
Sapra, K. Tanuj., Damaghi, M., Köster, S., Yildiz, Ö., Kühlbrandt, W. and Muller, Daniel J. (2009), One β Hairpin after the Other: Exploring Mechanical Unfolding Pathways of the Transmembrane β-Barrel Protein OmpG. Angew. Chem. Int. Ed., 48: 8306–8308. doi: 10.1002/anie.200904361
This work was supported by the Deutsche Forschungsgemeinschaft (grant nos.: YI 96/3-1 and MU 1791) and the European Union (ITN-SBMP). We thank C. Bippes and S. Mari for assistance and critical reading.
- Issue published online: 13 OCT 2009
- Article first published online: 28 SEP 2009
- Manuscript Received: 5 AUG 2009
- Deutsche Forschungsgemeinschaft. Grant Numbers: YI 96/3-1, MU 1791
- European Union
- barrel structures;
- mechanical unfolding;
- membrane proteins;
- molecular interactions;
- protein unfolding
Roll out the barrel: By using single-molecule force spectroscopy, a β-barrel-forming outer-membrane protein is unfolded for the first time. OmpG from E. coli shows a surprising unfolding behavior: Single β strands do not unfold individually but as β hairpins. These β hairpins unfold one after another until the entire β-barrel membrane protein is unfolded (see structural representation).