One β hairpin follows the other: Exploring refolding pathways and kinetics of the transmembrane β-barrel protein OmpG
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
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.
Details
Original language | English |
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Pages (from-to) | 7422-7424 |
Number of pages | 3 |
Journal | Angewandte Chemie - International Edition |
Volume | 50 |
Issue number | 32 |
Publication status | Published - 1 Aug 2011 |
Peer-reviewed | Yes |
External IDs
PubMed | 21692155 |
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Keywords
ASJC Scopus subject areas
Keywords
- β hairpins, mechanical unfolding, membrane proteins, protein folding, single-molecule force spectroscopy