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

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.

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 Creators:
Damaghi, Mehdi1, Author
Köster, Stefan2, Author           
Bippes, Christian A.1, Author
Yildiz, Özkan2, Author                 
Müller, Daniel J.1, Author
Affiliations:
1ETH Zürich, Department of Biosystems Science and Engineering, Basel, Switzerland, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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Free keywords: b hairpins; mechanical unfolding; membrane proteins; protein folding; single-molecule force spectroscopy
 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.

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Language(s): eng - English
 Dates: 2011-05-102011-02-272011-06-202011-08-01
 Publication Status: Issued
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201101450
PMID: 21692155
 Degree: -

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Title: Angewandte Chemie, International Edition in English
  Abbreviation : Angew. Chem., Int. Ed. Engl.
Source Genre: Journal
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Affiliations:
Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 50 (32) Sequence Number: - Start / End Page: 7422 - 7424 Identifier: ISSN: 0570-0833
CoNE: https://pure.mpg.de/cone/journals/resource/0570-0833