Science · 1992 · 203 citations · 20 references
BiochemistryProtein AssemblyProtein FoldingBiocatalysisBioenergeticsNatural SciencesProlyl IsomeraseMolecular BiologyMedicineEnzyme CatalysisProtein RefoldingCarbonic AnhydraseStructure-function Enzyme KineticsChemical BiologyProteomicsEnzymatic ModificationIsomerase ActivityChaperone Activity
Several proteins have been discovered that either catalyze slow protein-folding reactions or assist folding in the cell. Prolyl isomerase, which has been shown to accelerate rate-limiting cis-trans peptidyl-proline isomerization steps in the folding pathway, can also participate in the protein-folding process as a chaperone. This function is exerted on an early folding intermediate of carbonic anhydrase, which is thereby prevented from aggregating, whereas the isomerase activity is performed later in the folding process.
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Peptide-binding specificity of the molecular chaperone BiP
Gregory C. Flynn, Jan Pohl, Mark T. Flocco et al. · Nature · 1991 · 773 citations