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-literature | 2014 Nov

REPOSITORIES: biostudies-literature