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One β Hairpin after the Other: Exploring Mechanical Unfolding Pathways of the Transmembrane β‐Barrel Protein OmpG
Author(s) -
Sapra K. Tanuj,
Damaghi Mehdi,
Köster Stefan,
Yildiz Özkan,
Kühlbrandt Werner,
Muller Daniel J.
Publication year - 2009
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.200904361
Subject(s) - barrel (horology) , force spectroscopy , transmembrane protein , biophysics , membrane , unfolded protein response , chemistry , crystallography , bacterial outer membrane , molecule , materials science , biology , biochemistry , escherichia coli , endoplasmic reticulum , gene , composite material , receptor , organic chemistry
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).