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Related Experiment Videos

Protein thiol-disulfide interchange and interfacing with biological systems.

D B Wetlaufer, V P Saxena, A K Ahmed

    Advances in Experimental Medicine and Biology
    |January 1, 1977
    PubMed
    Summary

    Disulfide bonds in proteins aid structural studies. Uncatalyzed thiol-disulfide exchange, using glutathione (GSH) and oxidized glutathione (GSSG), is as effective as enzyme catalysis for protein folding.

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    Area of Science:

    • Biochemistry
    • Protein Folding
    • Chemical Kinetics

    Background:

    • Disulfide-containing proteins are valuable for studying the formation of native three-dimensional structures from reduced precursors.
    • Covalent intermediates in protein folding provide insights into reaction pathways.
    • Thiol-disulfide interchange is a key reaction in oxidative protein folding mechanisms.

    Purpose of the Study:

    • To investigate the rates of uncatalyzed thiol-disulfide exchange under physiologically relevant conditions.
    • To compare the efficiency of uncatalyzed exchange with enzyme-catalyzed ('shuffle-ase') mechanisms.
    • To understand the role of uncatalyzed reactions in biological thiol oxidations.

    Main Methods:

    • Studying the kinetics of protein folding.

    Related Experiment Videos

  • Utilizing glutathione (GSH) and oxidized glutathione (GSSG) systems.
  • Examining uncatalyzed thiol-disulfide exchange reactions.

    • Main Results:

    • Uncatalyzed thiol-disulfide exchange in GSH/GSSG systems demonstrated significant rates for native protein formation.
    • The rates of uncatalyzed protein folding were comparable to those observed with a 'shuffle-ase' enzyme.
    • These findings suggest a substantial contribution of uncatalyzed exchange to biological thiol oxidations.

    Conclusions:

    • Uncatalyzed thiol-disulfide exchange plays a significant role in the folding of native proteins.
    • Enzymatic catalysis may not be essential for all biological thiol oxidations.
    • Thiol-disulfide exchange, when linked to other redox systems, can achieve net oxidation level changes.