Targeted Quantification of Phosphopeptides by Parallel Reaction Monitoring (PRM)

Sara Christina Stolze; Hirofumi Nakagami

doi:10.1007/978-1-0716-0528-8_16

Targeted Quantification of Phosphopeptides by Parallel Reaction Monitoring (PRM)

Methods Mol Biol. 2020:2139:213-224. doi: 10.1007/978-1-0716-0528-8_16.

Authors

Sara Christina Stolze¹, Hirofumi Nakagami²

Affiliations

¹ Protein Mass Spectrometry Group, Max Planck Institute for Plant Breeding Research, Cologne, Germany.
² Protein Mass Spectrometry Group, Max Planck Institute for Plant Breeding Research, Cologne, Germany. nakagami@mpipz.mpg.de.

PMID: 32462589
DOI: 10.1007/978-1-0716-0528-8_16

Abstract

Parallel reaction monitoring (PRM) is a liquid chromatography-mass spectrometry (LC-MS)-based targeted peptide/protein quantification method that was initially implemented for Orbitrap mass spectrometers. Here, we describe detailed workflows that utilize the freely available MaxQuant and Skyline software packages to target peptides of interest, primarily focusing on phosphopeptides.

Keywords: Orbitrap mass spectrometer; Parallel reaction monitoring (PRM); Phosphopeptide; Phosphorylation; Posttranslational modification (PTM); Targeted quantification.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Chromatography, Liquid / methods*
Mass Spectrometry / methods*
Peptides / metabolism
Phosphopeptides / metabolism*
Proteins / metabolism
Proteomics / methods

Substances

Peptides
Phosphopeptides
Proteins