1999
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
Weber-Ban E, Reid B, Miranker A, Horwich A. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 1999, 401: 90-93. PMID: 10485712, DOI: 10.1038/43481.Peer-Reviewed Original ResearchConceptsSubstrate proteinsATP-dependent degradationGreen fluorescent protein GFPHydrogen exchange experimentsStable monomeric proteinFluorescent protein GFPNon-native formsChaperone ClpAChaperone familyEukaryotic proteinsProtease ClpPPresence of ATPChaperonin GroELHexameric ringClpAProteasome functionProtein GFPProtein structureMonomeric proteinNative proteinGlobal unfoldingProteinCentral channelRecognition peptideClpAP
1991
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
Martin J, Langer T, Boteva R, Schramel A, Horwich A, Hartl F. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 1991, 352: 36-42. PMID: 1676490, DOI: 10.1038/352036a0.Peer-Reviewed Original ResearchConceptsChaperonin-mediated proteinMolten globule-like intermediateMolten globule stateGroEL proteinProtein monomersMonomeric enzymeProtein structureTertiary structureATP moleculesGlobule stateGeneral mechanismMg-ATPGroESGroELFoldingProteinActive processPolypeptideEnzymeChain foldingConformationVivo