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One β Hairpin Follows the Other: Exploring Refolding Pathways and Kinetics of the Transmembrane β‐Barrel Protein OmpG
Author(s) -
Damaghi Mehdi,
Köster Stefan,
Bippes Christian A.,
Yildiz Özkan,
Müller Daniel J.
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201101450
Subject(s) - barrel (horology) , transmembrane protein , folding (dsp implementation) , chemistry , membrane , kinetics , biophysics , protein folding , membrane protein , computational biology , biochemistry , biology , materials science , physics , receptor , quantum mechanics , electrical engineering , composite material , engineering
One by one : 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 (see picture). This mechanism significantly advances the understanding of current folding models of β‐barrel proteins.
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