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Peptide Identification Using Tandem Mass Spectrometry

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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Related Experiment Video

Updated: Nov 21, 2025

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Advances in quantitative high-throughput phosphoproteomics with sample multiplexing.

Joao A Paulo¹, Devin K Schweppe²

¹Harvard Medical School, Boston, Massachusetts, USA.

|January 17, 2021

Summary

This summary is machine-generated.

This review explores advancements in quantitative phosphoproteomics, focusing on isobaric tag methods. It highlights challenges and future directions for analyzing cellular signaling pathways and their role in disease.

Keywords:

automation high-throughput tandem-mass tag

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Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Published on: August 2, 2018

Area of Science:

Molecular Biology
Biochemistry
Proteomics

Background:

Eukaryotic protein phosphorylation is crucial for biological processes, regulating protein activity and signal transduction.
Dysregulation of phosphorylation pathways is implicated in numerous diseases.
Mass spectrometry-based proteomics is vital for studying phosphoproteome perturbations.

Purpose of the Study:

To review current methodologies in quantitative phosphoproteomics.
To explore challenges in phosphoproteomic analysis.
To discuss the future outlook for isobaric tag-based quantitative phosphoproteomics.

Main Methods:

Advanced LC-MS/MS techniques for sensitive detection and localization of phosphorylation sites.
High-specificity enrichment strategies for phosphoproteome analysis.
Sample multiplexing using isobaric tags for enhanced throughput and sensitivity.

Main Results:

Isobaric tag-based quantitative phosphoproteomics offers advancements in throughput and sensitivity.
Current strategies require high-specificity enrichment, sensitive detection, and accurate localization.
Each aspect of phosphoproteomics presents unique challenges and opportunities for innovation.

Conclusions:

Quantitative phosphoproteomics, particularly with isobaric tags, is a powerful tool for understanding cellular signaling.
Addressing current challenges will drive innovation in the field.
Further development is needed to fully leverage phosphoproteomics for disease research.