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Updated: Jun 23, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
Protein folding in Escherichia coli: the chaperonin GroE and its substrates
Millicent Masters1, Garry Blakely, Andrew Coulson
1Institute of Cell Biology, University of Edinburgh, Kings Buildings, Edinburgh EH93JR, Scotland, United Kingdom. m.masters@ed.ac.uk
Abstract:
A brief summary of the role of DnaK and GroE chaperones in protein folding precedes a discussion of the role of GroE in Escherichia coli. We consider its obligate substrates, the 8 that are both obligate and essential, and the prospects for constructing a mutant that could survive without it. Structural features of GroE-dependent polypeptides are also considered.
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