1998
[11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL
Horwich A, Burston S, Rye H, Weissman J, Fenton W. [11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL. Methods In Enzymology 1998, 290: 141-146. PMID: 9534157, DOI: 10.1016/s0076-6879(98)90013-1.Peer-Reviewed Original ResearchConceptsBacterial chaperonin GroELGreen fluorescent proteinChaperonin GroELDouble-ring assemblyAddition of GroESDouble-ring complexesSingle-ring versionUnliganded GroELBacterial chaperoninsGroEL ringNeighboring subunitProtein foldsGroELEquatorial domainNonnative formsFluorescent proteinGroESNative stateNative formCentral channelCritical signalingSubunitsSignalingForm contactsNormal ATP
1996
Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction
Weissman J, Rye H, Fenton W, Beechem J, Horwich A. Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction. Cell 1996, 84: 481-490. PMID: 8608602, DOI: 10.1016/s0092-8674(00)81293-3.Peer-Reviewed Original ResearchConceptsCis ternary complexProtein foldingRelease of GroESAddition of GroESFolding reactionTernary complexNonhydrolyzable ATP analogGroES releaseProtein folding reactionSubstrate proteinsPresence of ATPGroEL mutantGroEL-GroESGroEL complexNonnative substratesATP hydrolysisGroESComplete foldingSubstrate flexibilityATP analogFoldingFluorescence anisotropyActive stateATPRecent studies