Jump to main content
Jump to site search

Issue 43, 2014
Previous Article Next Article

Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase

Author affiliations

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.

Graphical abstract: Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase

Back to tab navigation

Supplementary files

Publication details

The article was received on 14 Aug 2014, accepted on 17 Sep 2014 and first published on 18 Sep 2014


Article type: Communication
DOI: 10.1039/C4OB01738B
Author version available: Download Author version (PDF)
Citation: Org. Biomol. Chem., 2014,12, 8598-8602
  •   Request permissions

    Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase

    J. C. Lukesh III, K. A. Andersen, K. K. Wallin and R. T. Raines, Org. Biomol. Chem., 2014, 12, 8598
    DOI: 10.1039/C4OB01738B

Search articles by author

Spotlight

Advertisements