Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins |
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| Authors: | Saibil H |
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| Affiliation: | Department of Crystallography, Birkbeck College, London, WC1E 7HX, UK. H.Saibil@mail.cryst.bbk.ac.uk |
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| 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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