title: Molecular chaperones: inside and outside the Anfinsen cage.
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.
authors.affiliation: Department of Biological Sciences, University of Warwick, CV4 7AL, Coventry, UK. jellis@bio.warwick.ac.uk
authors.forename: R J
authors.initials: RJ
authors.lastname: Ellis
mesh_terms: D018832:Molecular Chaperones / Q000378:metabolism*; D017510:Protein Folding; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism; D013884:Thiosulfate Sulfurtransferase / Q000378:metabolism
chemical_list: D018832:Molecular Chaperones; D013884:Thiosulfate Sulfurtransferase; D012273:Ribulose-Bisphosphate Carboxylase