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Updated: Jun 8, 2026
09:10
A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
Published on: May 22, 2018
Mapping of phosphorylation sites by LC-MS/MS
Bertran Gerrits1, Bernd Bodenmiller
1Functional Genomics Center Zurich, University of Zurich and Swiss Federal Institute of Technology, Zurich, Switzerland.
Methods in Molecular Biology (Clifton, N.J.)
|September 15, 2010
Summary
Reversible protein phosphorylation is crucial for cell function but hard to study due to low amounts. New enrichment techniques improve the analysis of phosphopeptides in complex biological samples.
Area of Science:
- Biochemistry
- Cell Biology
- Proteomics
Background:
- Reversible protein phosphorylation is a key post-translational modification regulating cellular processes.
- Studying phosphorylation is challenging due to the low stoichiometry of modified peptides.
- Standard LC-MS analysis has limitations in detecting low-abundance phosphopeptides.
Purpose of the Study:
- To address the challenges in analyzing protein phosphorylation.
- To present novel techniques for phosphopeptide enrichment.
- To facilitate large-scale analysis of phosphorylation states.
Main Methods:
- Development of specific enrichment strategies for phosphopeptides.
- Application of biochemical methods for isolating phosphorylated proteins.
- Utilizing advanced mass spectrometry techniques.
Main Results:
- Improved detection of low-stoichiometry phosphopeptides.
- Enhanced coverage of the phosphoproteome.
- Successful application of enrichment techniques in complex mixtures.
Conclusions:
- Specific enrichment methods are essential for accurate phosphoproteomic analysis.
- Advancements in phosphopeptide isolation enable deeper insights into cellular signaling.
- These techniques overcome limitations of standard mass spectrometry for phosphorylation studies.
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