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Characterizing Cellular Proteins with In-cell Fast Photochemical Oxidation of Proteins
Published on: March 11, 2020
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Oxidative Protein Folding Using trans-3,4-Dihydroxyselenolane Oxide.
1Department of Chemistry, School of Science, Tokai University, Hiratsuka-shi, Kanagawa, Japan.
Methods in Molecular Biology (Clifton, N.J.)
|May 10, 2019
Summary
trans-3,4-Dihydroxyselenolane oxide (DHSox) efficiently forms disulphide bonds in proteins. This selective oxidant aids in characterizing protein folding pathways and thiol reactivity, outperforming traditional reagents.
Area of Science:
- Biochemistry
- Protein Chemistry
- Chemical Biology
Background:
- Protein folding relies on precise disulfide bond formation.
- Existing reagents for disulfide bond formation have limitations in selectivity and application range.
- Characterizing oxidative folding pathways requires specific and efficient chemical tools.
Purpose of the Study:
- To introduce and demonstrate the utility of trans-3,4-Dihydroxyselenolane oxide (DHSox) as a novel reagent for protein studies.
- To highlight the advantages of DHSox over conventional disulfide bond-forming reagents.
- To showcase DHSox's application in analyzing protein folding intermediates and thiol reactivity.
Main Methods:
- Utilizing DHSox as a selective oxidant for thiol substrates (RSH).
- Applying DHSox for rapid and quantitative disulfide (SS) bond formation in proteins.
- Employing DHSox to diagnose protein structure, thiol pKa, and folding intermediates.
Main Results:
- DHSox enables efficient and quantitative disulfide bond formation across a wide pH range.
- DHSox demonstrates superior selectivity compared to oxidized dithiothreitol (DTTox) and glutathione (GSSG).
- DHSox facilitates the identification of key disulfide intermediates and the characterization of misfolded species.
Conclusions:
- DHSox is a versatile and powerful reagent for studying protein oxidative folding.
- The unique properties of DHSox offer significant advantages for protein characterization and analysis.
- DHSox provides new avenues for understanding complex protein folding dynamics and disulfide bond manipulation.
Keywords:
Disulphide formationDisulphide intermediatesKinetic analysisOxidation pulseOxidative folding pathwaysRedox potentialpH effectsMore Related Videos
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