STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING
Sigler P, Xu Z, Rye H, Burston S, Fenton W, Horwich A. STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING. Annual Review Of Biochemistry 1998, 67: 581-608. PMID: 9759498, DOI: 10.1146/annurev.biochem.67.1.581.Peer-Reviewed Original ResearchConceptsProtein foldingNative stateMechanism of chaperoninsCis ternary complexAsymmetric conformational changesFinal native stateNonnative polypeptidesCochaperonin GroESGroEL ringTrans ringATP hydrolysisGenetic informationChaperonin moleculesConformational changesFolding processFoldingTernary complexPolypeptideGroESATPBiochemical investigationsFinal stepChaperoninGroELComplexesChaperone Action in Folding Newly-Translated Cytosolic Proteins in Bacteria and Eukaryotes
Horwich A. Chaperone Action in Folding Newly-Translated Cytosolic Proteins in Bacteria and Eukaryotes. NATO ASI Series 1998, 41-63. DOI: 10.1007/978-3-642-51463-0_4.Peer-Reviewed Original ResearchNon-native conformationsNative statePrimary amino acid sequenceAmino acid sequenceNon-native statesSubstrate proteinsChaperone functionMolecular chaperonesBiogenesis stepsChaperone actionSpecialized proteinsCofactor bindingProtein foldingAction of nucleotidesPathway stepsMutational alterationsCytosolic proteinsAcid sequenceChaperonesSteric informationFolding processSuch hydrophobic interactionsProteinNative formEssential nature