Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 12, Issue 6, Pages 740-745Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2008.08.032
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Funding
- National Science Foundation [CHE-0342167]
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Oxidative protein folding occurs both in vivo and in vitro and involves the formation and rearrangement of protein disulfide bonds (-S-S- bonds). In vivo these reactions are catalyzed by enzymes, including the eukaryotic enzyme protein disulfide isomerase (PDI). Using the physical properties of PDI as a guide, several small-molecule catalysts of oxidative protein folding have been designed, synthesized, and tested. These small molecules can improve the folding rate of the model substrate ribonuclease A by a factor of over 10 and improve the yield by up to a factor of 3 over traditional conditions. The molecules have also been demonstrated to significantly improve the in vivo folding of proteins as well.
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