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Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...

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Related Experiment Video

Updated: Oct 17, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

SPEAR: A proteomics approach for simultaneous protein expression and redox analysis.

Shani Doron¹, Nardy Lampl¹, Alon Savidor²

¹The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, The Hebrew University of Jerusalem, Rehovot 7610000, Israel.

Free Radical Biology & Medicine

|October 7, 2021

Summary

This study introduces Simultaneous Protein Expression and Redox (SPEAR) analysis, a novel redox proteomics method. SPEAR efficiently quantifies cysteine oxidation states and protein abundance, revealing widespread redox regulation in plants.

Keywords:

Chloroplasts Cysteine Mass-spectrometry N-ethylmaleimide Plants Redox proteomics Redox regulation

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Last Updated: Oct 17, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

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Published on: June 21, 2021

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

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Published on: March 24, 2012

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Area of Science:

Plant Biology
Proteomics
Biochemistry

Background:

Protein cysteinyl thiol oxidation/reduction is a key mechanism for biological redox regulation.
Redox proteomics identifies and quantifies redox-modified cysteine sites, aiding mechanistic research.

Purpose of the Study:

To develop a novel redox proteomics approach for simultaneous quantification of cysteine oxidation state and protein abundance.
To investigate the dynamics of the redox proteome in Arabidopsis under varying conditions.

Main Methods:

Developed Simultaneous Protein Expression and Redox (SPEAR) analysis.
Utilized differential labeling of reversibly oxidized and reduced cysteines with isotopically-labeled N-ethylmaleimide (NEM).
Applied SPEAR to quantify in-vivo cysteine oxidation state and protein abundance in Arabidopsis proteome without peptide enrichment.

Main Results:

Quantified in-vivo reversible oxidation state of thousands of cysteines in Arabidopsis.
Demonstrated widespread effects of oxidative conditions on cellular functions, particularly in chloroplasts.
Identified both known and novel redox-sensitive sites.

Conclusions:

SPEAR analysis offers a simple, cost-effective method for studying redox proteome dynamics.
The findings provide a global quantitative view of reversible cysteine oxidation in plants.
Further research is needed to explore the role of novel redox-sensitive sites in plant stress acclimation.