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Updated: Feb 4, 2026

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
Thiol-Redox Proteomics to Study Reversible Protein Thiol Oxidations in Bacteria
Martina Rossius1, Falko Hochgräfe2, Haike Antelmann3
1Institute for Biology-Microbiology, Freie Universität Berlin, Berlin, Germany.
Abstract:
Thiol-redox proteomics methods are rapidly developing tools in redox biology. These are applied to identify and quantify proteins with reversible thiol oxidations that are formed under normal growth and oxidative stress conditions inside cells. The proteins with reversible thiol oxidations are usually prepared by alkylation of reduced thiols, subsequent reduction of disulfide bonds followed by a second differential alkylation of newly released thiols. Here, we describe two methods for detection of protein S-thiolations in Gram-positive bacteria using the direct shotgun approach and the fluorescent-label thiol-redox proteomics method that have been successfully applied in our previous work.
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