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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

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Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
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Cysteine tagging for MS-based proteomics.

Priscille Giron1, Loïc Dayon, Jean-Charles Sanchez

  • 1Biomedical Proteomics Research Group, Structural Biology and Bioinformatics Department, University of Geneva, Geneva, Switzerland.

Mass Spectrometry Reviews
|April 19, 2011
PubMed
Summary
This summary is machine-generated.

Mass tagging in proteomics utilizes labels for mass spectrometry (MS) analysis. This review focuses on cysteine-specific mass-tagging methods, highlighting their advantages and applications in MS-based proteomics.

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Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Mass spectrometry (MS) is central to protein sciences.
  • Mass tagging involves attaching labels to peptides/proteins for MS analysis.
  • Cysteine residues are frequent targets for modification due to their reactive thiol group.

Purpose of the Study:

  • To comprehensively review mass-tagging methods targeting cysteine residues.
  • To discuss the advantages and drawbacks of these cysteine-tagging strategies.
  • To illustrate the relevance of cysteine-tagging techniques in MS-based proteomics through applications.

Main Methods:

  • Review of existing literature on mass-tagging techniques.
  • Focus on methods specifically targeting cysteine residues.
  • Analysis of chemical reactivity of cysteine thiols for labeling.

Main Results:

  • Cysteine's unique properties make it an ideal target for mass tagging.
  • Various mass-tagging strategies directed to cysteine are discussed.
  • Advantages and disadvantages of different cysteine-tagging approaches are evaluated.

Conclusions:

  • Cysteine-tagging is a valuable approach in MS-based proteomics.
  • These methods enhance separation, enrichment, detection, and quantitation of peptides/proteins.
  • Targeting cysteine residues offers specific analytical advantages in proteomic studies.