1997
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
Goldberg M, Zhang J, Sondek S, Matthews C, Fox R, Horwich A. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 1080-1085. PMID: 9037009, PMCID: PMC19747, DOI: 10.1073/pnas.94.4.1080.Peer-Reviewed Original ResearchConceptsNative-like structureChaperonin GroELDihydrofolate reductaseProtein-folding intermediatesNative dihydrofolate reductaseStopped-flow fluorescence experimentsNonnative proteinsSubstrate proteinsProductive foldingPresence of ATPHuman dihydrofolate reductaseHydrogen-deuterium exchangeGroELPrimary structureProteinCentral channelHydrophobic interactionsFluorescence experimentsGroESFoldingSpeciesReductaseNMR spectroscopyDistant partsATP
1993
High-resolution gold labeling
Hainfeld J, Furuya F, Carbone K, Simon M, Lin B, Braig K, Horwich A, Safer D, Blechschmidt B, Sprinzl M, Ofengand J, Boublik M. High-resolution gold labeling. Microscopy And Microanalysis 1993, 51: 330-331. DOI: 10.1017/s0424820100147491.Peer-Reviewed Original ResearchGroEL complexDihydrofolate reductaseNascent polypeptide chainsChaperonin GroELMacromolecular complexesOligomeric complexesSmall proteinsActive proteinPolypeptide chainGroELChaperoninGold clustersCentral cavityGold labelingSpecific sitesGold compoundsModel substrateProteinMacromolecular sitesComplexesExternal surfaceRibosomesReductaseSitesChain