Abstract
Organocatalysts derived from diethylenetriamine effect the rapid isomerization of non-native protein disulfide bonds to native ones. These catalysts contain a pendant hydrophobic moiety to encourage interaction with the non-native state, and two thiol groups with low pKa values that form a disulfide bond with a high E°' value.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Catalysis
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Cattle
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Disulfides / chemistry*
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Isomerism
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Kinetics
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Molecular Mimicry
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Oxidation-Reduction
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Pancreas / chemistry
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Pancreas / enzymology
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Polyamines / chemistry*
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Protein Conformation
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Protein Disulfide-Isomerases / chemistry*
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Protein Folding
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Ribonuclease, Pancreatic / chemistry*
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Small Molecule Libraries / chemical synthesis*
Substances
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Disulfides
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Polyamines
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Small Molecule Libraries
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diethylenetriamine
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Ribonuclease, Pancreatic
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Protein Disulfide-Isomerases