Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins
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Updated: Oct 17, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
1Department of Crystallography, Birkbeck College, London, WC1E 7HX, UK. H.Saibil@mail.cryst.bbk.ac.uk
Abstract:
Newly solved chaperone structures include the thermosome, a group II chaperonin, and a small heat-shock protein. Novel ideas on chaperone mechanism are presented in the forced unfolding hypothesis of GroEL action. Structures of chaperone-pilin complexes reveal the mechanism of chaperone interaction in bacterial pilus assembly and there have been major advances in understanding the structure and function of Hsp100 unfoldases.
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