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Updated: Jul 26, 2026

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
The oxidative folding of proteins by disulfide plus thiol does not correlate with redox potential
D B Wetlaufer1, P A Branca, G X Chen
1Department of Chemistry, University of Delaware, Newark 19716.
Abstract:
The rate and yield of oxidative renaturation of reduced RNase A has been studied as a function of [-S-S-]/[-SH]. The principal conclusion of these studies is that rates and yields of oxidative renaturation are strongly dependent on the low mol. wt disulfide/thiol ratio. The relationships are complex and do not parallel the redox potential of the system. The present results are consistent with earlier findings on other proteins, and lead us to believe that the above conclusion is general. Kinetic studies of oxidative renaturation should recognize and account for the dependence of reaction rate and extent on the disulfide/thiol ratio. This ratio can change substantially over the course of a reaction, either due to stoichiometric transfer of disulfide to protein, and/or adventitious air oxidation of thiols. Failure to account for changes in the disulfide/thiol ratio may compromise the interpretation of such experiments.
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