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Journal Article

One β Hairpin Follows the Other: Exploring Refolding Pathways and Kinetics of the Transmembrane β-Barrel Protein OmpG

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Köster,  Stefan
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Yildiz,  Özkan       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Damaghi, M., Köster, S., Bippes, C. A., Yildiz, Ö., & Müller, D. J. (2011). One β Hairpin Follows the Other: Exploring Refolding Pathways and Kinetics of the Transmembrane β-Barrel Protein OmpG. Angewandte Chemie, International Edition in English, 50(32), 7422-7424. doi:10.1002/anie.201101450.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D630-3
Abstract
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. This mechanism significantly advances the understanding of current folding models of β-barrel proteins.