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Molecular chaperones: Inside and outside the Anfinsen cage
Authors:RJohn Ellis  
Institution: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.
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