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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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Updated: Mar 8, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Computational and Statistical Methods for High-Throughput Mass Spectrometry-Based PTM Analysis.

Veit Schwämmle¹, Marc Vaudel²

¹Protein Research Group, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, 5230, Odense, Denmark. veits@bmb.sdu.dk.

Methods in Molecular Biology (Clifton, N.J.)

|February 3, 2017

Summary

This summary is machine-generated.

Characterizing protein post-translational modifications (PTMs) is crucial for understanding cell functions. This study presents a workflow to interpret complex mass spectrometry data, aiding biological and medical research.

Keywords:

Bioinformatics Post-translational modifications (PTMs)Proteomics

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Area of Science:

Proteomics
Biochemistry
Molecular Biology

Background:

Post-translational modifications (PTMs) are critical for protein function and cell signaling.
High-throughput characterization of PTMs is essential for biological and medical research.
Mass spectrometry is a powerful tool for quantitative proteomic analysis.

Purpose of the Study:

To present a typical workflow for interpreting complex peptide mass spectrometry data.
To address the challenges associated with large-scale PTM data analysis.
To facilitate quantitative comparisons of modified peptides across different experimental conditions.

Main Methods:

Peptide mass spectrometry analysis.
Efficient enrichment methods for modified peptides.
Data interpretation workflow including spectral analysis and statistical methods.

Main Results:

A comprehensive workflow for interpreting large and complex post-translational modification datasets.
Enables quantitative comparison of thousands of modified peptides.
Addresses challenges in spectral interpretation and multivariate analysis.

Conclusions:

The presented workflow aids in the interpretation of complex proteomic data.
Facilitates a deeper understanding of protein function and cell signaling through PTM analysis.
Supports high-throughput characterization of PTMs for biological and medical investigations.