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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

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: Jun 8, 2026

Large-scale Top-down Proteomics Using Capillary Zone Electrophoresis Tandem Mass Spectrometry
10:05

Large-scale Top-down Proteomics Using Capillary Zone Electrophoresis Tandem Mass Spectrometry

Published on: October 24, 2018

A Protocol for top-down proteomics using HPLC and ETD/PTR-MS.

Sarah R Hart1

  • 1Michael Barber Centre for Mass Spectrometry, University of Manchester, Manchester, UK.

Methods in Molecular Biology (Clifton, N.J.)
|September 15, 2010
PubMed
Summary
This summary is machine-generated.

This study presents a novel protocol for analyzing intact proteins using tandem mass spectrometry, making the technique accessible beyond high-end platforms. It combines routine HPLC, MALDI-ToF, and electron transfer dissociation for comprehensive protein analysis.

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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
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Last Updated: Jun 8, 2026

Large-scale Top-down Proteomics Using Capillary Zone Electrophoresis Tandem Mass Spectrometry
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Published on: October 24, 2018

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

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

Published on: November 15, 2017

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Intact protein analysis via tandem mass spectrometry (MS/MS) is typically limited to specialized, high-cost instrumentation.
  • There is a need for accessible methods to perform intact protein analysis.

Purpose of the Study:

  • To describe a protocol for intact protein analysis using tandem mass spectrometry on routine laboratory equipment.
  • To enable broader application of intact protein MS/MS.

Main Methods:

  • Utilized High-Performance Liquid Chromatography (HPLC) for protein separation.
  • Employed Matrix-Assisted Laser Desorption/Ionization Time-of-Flight (MALDI-ToF) mass spectrometry to analyze intact protein species.
  • Implemented electron transfer dissociation (ETD) and proton transfer reaction (PTR) within a quadrupole ion trap for tandem mass spectrometry.

Main Results:

  • Successfully applied routine HPLC for protein separation prior to mass spectrometry analysis.
  • Demonstrated the interrogation of intact protein species using MALDI-ToF MS.
  • Showcased the capability of ETD/PTR in a quadrupole ion trap for performing tandem mass spectrometry on intact proteins.

Conclusions:

  • This protocol democratizes intact protein analysis by leveraging standard HPLC and MALDI-ToF MS platforms.
  • The described method provides a viable alternative for tandem mass spectrometry analysis of intact proteins without requiring ultra-high-end instruments.