One β Hairpin after the Other: Exploring Mechanical Unfolding Pathways of the 
Transmembrane β-Barrel Protein OmpG

Sapra, K. Tanuj; Damaghi, Mehdi; Köster, Stefan; Yildiz, Özkan; Kühlbrandt, Werner; Muller, Daniel J.

doi:10.1002/anie.200904361

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One β Hairpin after the Other: Exploring Mechanical Unfolding Pathways 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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引用

Sapra, K. T., Damaghi, M., Köster, S., Yildiz, Ö., Kühlbrandt, W., & Muller, D. J. (2009). One β Hairpin after the Other: Exploring Mechanical Unfolding Pathways of the Transmembrane β-Barrel Protein OmpG. Angewandte Chemie, International Edition in English, 48(44), 8306-8308. doi:10.1002/anie.200904361.

引用: https://hdl.handle.net/11858/00-001M-0000-0024-D7A9-B

要旨

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).