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Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase.


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.

SUBMITTER: Lukesh JC 

PROVIDER: S-EPMC4237591 | biostudies-other | 2014 Nov

REPOSITORIES: biostudies-other

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Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase.

Lukesh John C JC   Andersen Kristen A KA   Wallin Kelly K KK   Raines Ronald T RT  

Organic & biomolecular chemistry 20141101 43


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. ...[more]

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