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Related Concept Videos

Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

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Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Related Experiment Video

Updated: Jul 28, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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Thiol redox proteomics: Characterization of thiol-based post-translational modifications.

Xiaolu Li1, Austin Gluth1,2, Tong Zhang1

  • 1Biological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington, USA.

Proteomics
|May 30, 2023
PubMed
Summary

Redox post-translational modifications (PTMs) regulate biological processes. Advanced redox proteomics, utilizing mass spectrometry, now allows for comprehensive analysis of these critical protein changes.

Keywords:
cysteinepost-translational modificationsprotein thiolsredox PTMsredox proteomicsthiol redox proteome

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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Redox post-translational modifications (PTMs) on cysteine thiols significantly impact protein structure and function.
  • These modifications are crucial for regulating diverse biological processes and cellular signaling pathways.
  • Understanding redox PTMs is key to deciphering cellular regulation and disease mechanisms.

Purpose of the Study:

  • To review the principles and recent advances in redox proteomics.
  • To highlight analytical strategies for characterizing redox PTMs.
  • To illustrate the application of redox proteomics in gaining biological insights.

Main Methods:

  • Discusses established thiol-blocking and selective reduction strategies.
  • Covers novel chemoselective probe-based approaches for various redox PTMs.
  • Includes direct detection methods enabled by sensitive mass spectrometry (MS).

Main Results:

  • Significant advances in redox proteomics have been made in the last decade.
  • Various analytical strategies, including enrichment and direct detection, are available.
  • Large-scale redox proteomics data provide novel biological insights.

Conclusions:

  • Redox proteomics is a powerful systems-level approach to study redox PTMs.
  • Advances in MS have enhanced the sensitivity and scope of redox proteomics.
  • This field continues to deepen our understanding of redox signaling and regulation.