A polypeptide bound by the chaperonin groEL is localized within a central cavity.
Braig K, Simon M, Furuya F, Hainfeld J, Horwich A. A polypeptide bound by the chaperonin groEL is localized within a central cavity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 3978-3982. PMID: 8097882, PMCID: PMC46429, DOI: 10.1073/pnas.90.9.3978.Peer-Reviewed Original ResearchConceptsChaperonin GroELGroEL complexEscherichia coli chaperonin GroELOligomeric protein complexesDihydrofolate reductaseMolten globule-like intermediateCentral cavityPolypeptide chain foldingChaperonin ringsChaperonin complexProtein complexesCellular compartmentsDHFR moleculeMonomeric membersPresence of MgATPGroELNative stateEssential roleCompact conformationPolypeptideComplexesCochaperoninChaperoninMultiple sitesIntermediatesProtein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1
Horwich A, Willison K. Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1. Philosophical Transactions Of The Royal Society B Biological Sciences 1993, 339: 313-326. PMID: 8098536, DOI: 10.1098/rstb.1993.0030.Peer-Reviewed Original ResearchProtein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1
Horwich A, Willison K. Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1. 1993, 57-70. DOI: 10.1007/978-94-011-2108-8_8.Peer-Reviewed Original Research