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Phosphorylation

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

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Related Experiment Video

Updated: Apr 19, 2026

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

[In vitro protein phosphorylation as a template for SRM method development].

M G Zav'ialova¹, V G Zgoda¹, O N Kharybin¹

¹Orekhovich Institute of Biomedical Chemistry (IBMC).

Biomeditsinskaia Khimiia

|January 2, 2015

Summary

Detecting low-abundance phosphoproteins like myelin basic protein (MBP) is challenging. We developed a sensitive selected reactions monitoring (SRM) method using a kinase system and MBP as a template, successfully detecting phosphopeptides in glioma samples.

Keywords:

post-translational modifications (PTM)protein phosphorylation proteomics selected reaction monitoring (SRM)

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Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

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Published on: June 30, 2019

Related Experiment Videos

Last Updated: Apr 19, 2026

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Area of Science:

Biochemistry
Proteomics
Molecular Biology

Context:

Phosphorylation is a crucial post-translational modification (PTM) regulating protein function.
Detecting low-abundance phosphoproteins presents a significant analytical challenge in proteomics.
Selected Reactions Monitoring (SRM) offers high sensitivity and selectivity for targeted peptide analysis.

Purpose:

To develop a robust method for sensitive phosphoprotein detection using SRM.
To establish a workflow for generating phosphorylated protein templates for SRM assay development.
To validate the developed method for detecting specific phosphopeptides in complex biological samples.

Summary:

A novel method for phosphoprotein detection was developed using myelin basic protein (MBP) as a model system.
The approach involves reconstituting MBP phosphorylation in vitro and utilizing the resulting phosphoprotein to generate a targeted SRM assay.
This method enables sensitive and selective detection of phosphopeptides, overcoming the challenge of low endogenous phosphoprotein abundance.

Impact:

The developed SRM method facilitates the sensitive detection of phosphoproteins, even when present at low levels.
This technique can be applied to study the role of specific phosphorylation events in various biological processes and diseases.
Successful application in human brain glioma samples demonstrates the method's potential for clinical biomarker discovery.