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Updated: Aug 11, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
Protein folding and unfolding by Escherichia coli chaperones and chaperonins
M E Gottesman1, W A Hendrickson
1Departments of Microbiology and of Biochemistry and Molecular Biophysics, Institute of Cancer Research, Columbia University, New York, NY 10032, USA. gottesman@cuccfa.ccc.columbia.edu
Abstract:
The folding of proteins from their initial unstructured state to their mature form has long been known to be promoted by other proteins known as chaperones and chaperonins. Recent biochemical and structural discoveries have provided dramatic insight into how these folding proteins work. This review will discuss these findings and suggest future experimental directions.
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