Catalysis of protein folding by prolyl isomerase
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Abstract
References (16)
Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
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Specific Intermediates in the Folding Reactions of Small Proteins and the Mechanism of Protein Folding
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The Preparation of Subtilisin-modified Ribonuclease and the Separation of the Peptide and Protein Components
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Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerization
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Both the Fast and Slow Refolding Reactions of Ribonuclease A Yield Native Enzyme
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Unfolding and refolding of the constant fragment of the immunoglobulin light chain
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The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomerase
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Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease.
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The Primary Structure of Porcine Pancreatic Ribonuclease
1970 • 81 citations
Identification and characterization of the direct folding process of hen egg-white lysozyme
1982 • 65 citations
Involvement of prolines-114 and -117 in the slow refolding phase of ribonuclease A as determined by isomer-specific proteolysis
1984 • 59 citations
Mechanism for the unfolding and refolding of ribonuclease A. Simulations using a simple model with no structural intermediates
1983 • 43 citations
Recombination of S-peptide with S-protein during folding of ribonuclease S
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Folding mechanism of porcine ribonuclease
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