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Curr Biol. 2001 Dec 11;11(24):R1038-40.

Molecular chaperones: inside and outside the Anfinsen cage.

Author information

1
Department of Biological Sciences, University of Warwick, CV4 7AL, Coventry, UK. jellis@bio.warwick.ac.uk

Abstract

The GroEL/GroES chaperonin system acts as a passive anti-aggregation cage for refolding rubisco and rhodanese, and not as an active unfolding device. Refolding aconitase is too large to enter the cage but reversible binding to GroEL reduces its aggregration. Unexpectedly, confinement in the cage increases the rate of refolding of rubisco, but not rhodanese.

PMID:
11747844
DOI:
10.1016/s0960-9822(01)00620-0
[Indexed for MEDLINE]
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