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Updated: Oct 6, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
La cage aux fold: asymmetry in the crystal structure of GroEL-GroES-(ADP)7
1Laboratories of Molecular Biophysics, Howard Hughes Medical Institute, Rockefeller University, NY 10021, USA. harrice@rockvax.rockefeller.edu
Abstract:
The structure of the molecular chaperone GroEL from Escherichia coli in complex with GroES and seven ADP molecules has recently been reported to 3 A resolution. The structure illustrates how the cavity of GroEL is converted from a hydrophobic environment, suitable for binding unfolded polypeptides, to a much larger hydrophilic environment suitable for refolding proteins.
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