One-step refolding and purification of disulfide-containing proteins with a C-terminal MESNA thioester
2008
New Method for Refolding Proteins with Thioesters
publication
Evidence: moderate
Author Information
Author(s): Bastings Maartje MC, van Baal Ingrid, Meijer EW, Merkx Maarten
Primary Institution: Eindhoven University of Technology
Hypothesis
Can a new redox buffer improve the refolding of disulfide-containing proteins while preserving thioester functionality?
Conclusion
A novel method was developed for the production of disulfide bond containing proteins with C-terminal thioesters.
Supporting Evidence
- The MESNA/diMESNA redox couple showed comparable refolding efficiency to glutathione.
- The method allowed simultaneous on-column refolding and thioester generation.
- Active RNase A was produced using the new refolding strategy.
Takeaway
Scientists created a new way to help proteins fold correctly while keeping a special part that helps them stick to other things.
Methodology
The study developed a MESNA/diMESNA redox buffer for simultaneous refolding and purification of proteins.
Digital Object Identifier (DOI)
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