These authors contributed equally to this work.
1521-3773/asset/2002_left.gif?v=1&s=ac6b0d94a94d7ce7a210002b8096b42feffc0bcf)
1521-3773/asset/olbannercenter.gif?v=1&s=c083e1920cd41ed129901c116018eab93b5ad3c4)
1521-3773/asset/2002_right.gif?v=1&s=451042aa3415ae3ad0729984d26dee1866aca82e)
Communication
One β Hairpin after the Other: Exploring Mechanical Unfolding Pathways of the Transmembrane β-Barrel Protein OmpG†
Article first published online: 28 SEP 2009
DOI: 10.1002/anie.200904361
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
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.
- ‡
These authors contributed equally to this work.
Publication History
- Issue published online: 13 OCT 2009
- Article first published online: 28 SEP 2009
- Manuscript Received: 5 AUG 2009
Funded by
- Deutsche Forschungsgemeinschaft. Grant Numbers: YI 96/3-1, MU 1791
- European Union
Keywords:
- 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).