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Mass spectrometry-based quantitative proteomic profiling.

Wei Yan1, Sharon S Chen

  • 1Institute for Systems Biology, 1441 N. 34th Street, Seattle, WA 98103-8904, USA. wyan@systemsbiology.org

Briefings in Functional Genomics & Proteomics
|June 25, 2005
PubMed
Summary
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Quantitative proteomics uses stable isotope labeling for protein analysis. New methods enable multiplexing and improved mass spectrometry, simplifying complex proteomes through sub-proteome fractionation for deeper insights.

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Systems Biology

Background:

  • Quantitative proteomics is crucial for understanding biological systems.
  • Stable isotope labeling (metabolic and chemical) is a primary method for global proteome profiling.
  • Advancements include multiplexing capabilities and ion intensity-based quantification.

Purpose of the Study:

  • To review the current state and challenges in quantitative proteomics.
  • To highlight the role of stable isotope labeling and mass spectrometry advancements.
  • To discuss the potential of sub-proteome fractionation for comprehensive proteome analysis.

Main Methods:

  • Stable isotope labeling (metabolic and chemical) for protein quantitation.
  • Mass spectrometry (MS) for identification and quantification.

Related Experiment Videos

  • Sub-proteome fractionation techniques to simplify complex samples.

    • Main Results:

    • Stable isotope labeling has evolved to allow multiplex sample quantification.
    • Improved mass spectrometry enhances ion intensity-based quantitative approaches.
    • Sub-proteome fractionation simplifies proteome complexity, aiding comprehensive characterization.

    Conclusions:

    • Despite advancements, comprehensive proteome characterization remains challenging due to complexity and dynamic range.
    • Sub-proteome fractionation is a key strategy for simplifying the proteome.
    • Future developments will focus on intelligent, functional targeting of sub-proteomes for advanced analysis.