1997
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
Rye H, Burston S, Fenton W, Beechem J, Xu Z, Sigler P, Horwich A. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 1997, 388: 792-798. PMID: 9285593, DOI: 10.1038/42047.Peer-Reviewed Original ResearchConceptsTrans ringProductive foldingGroES complexChaperonin GroELCis ringCo-chaperone GroESDouble-ring complexesCis ternary complexNon-hydrolysable ATPHydrolysis of ATPGroEL functionGroEL-ATPATP bindingEfficient foldingBinds ATPATP hydrolysisGroESMutant formsMalate dehydrogenaseGroELAMP-PNPDouble-ring structureFoldingTernary complexATP
1994
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
Weissman J, Kashi Y, Fenton W, Horwich A. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell 1994, 78: 693-702. PMID: 7915201, DOI: 10.1016/0092-8674(94)90533-9.Peer-Reviewed Original ResearchConceptsCochaperonin GroESMultiple roundsGroEL functionChaperonin GroELKinetic partitioningMutant formsNonnative conformationsNonnative formsGroELAddition of ATPGroEL moleculeTryptophan fluorescenceFolding reactionDouble-ring structureUnfolded statePolypeptideDiverse setGroESProteolysisProteinATPBindingFateConformationComplexes