Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

6.5K
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...
6.5K
Mass Analyzers: Common Types01:19

Mass Analyzers: Common Types

620
The quadrupole mass analyzer consists of four cylindrical metal rods arranged in a diamond carrying a DC voltage and a radio-frequency AC voltage. The motion of ions through the quadrupole depends on the field strength, causing only ions of a certain m/z to resonate successfully and strike the detector at a given field strength. Though the transmission rate for these analyzers is high, the exact elemental composition of the sample is not determined because of low resolution; however, they are...
620
Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

800
Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
800

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

An Amphibious Bifunctional Probe for Protein Chemical Cross-Linking.

Journal of the American Chemical Society·2026
Same author

De novo EHMT2 variants cause an autosomal dominant EHMT2-related Kleefstra syndrome via loss of G9a methyltransferase activity.

Nature communications·2026
Same author

The Rise of Trapped Ion Mobility Spectrometry: Principles, Applications, and Recent Developments.

Mass spectrometry reviews·2026
Same author

Cytotoxic Synurins A-C: Chlorinated Naphthoquinone Pigments from the Freshwater Alga <i>Synura sphagnicola</i>.

Journal of natural products·2026
Same author

Recommendations and considerations for hydroxyl radical protein footprinting-mass spectrometry.

Nature methods·2026
Same author

Online Deglycosylation of Monomeric Intact Proteins Using the PNGase Rc Immobilized-Enzyme Reactor.

ACS omega·2026

Related Experiment Video

Updated: Jul 12, 2025

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

9.5K

Top-Down Proteoform Analysis by 2D MS with Quadrupolar Detection.

Marek Polák1,2, Michael Palasser3, Alan Kádek1

  • 1Institute of Microbiology of the Czech Academy of Sciences, Prague 14220, Czech Republic.

Analytical Chemistry
|October 25, 2023
PubMed
Summary
This summary is machine-generated.

Two-dimensional mass spectrometry (2D MS) with quadrupolar detection in a harmonized ICR cell enables comprehensive fragmentation analysis without ion isolation. This advancement allows for detailed biomolecule studies and label-free quantification.

More Related Videos

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

12.0K
Quantitative Proteomics Workflow using Multiple Reaction Monitoring Based Detection of Proteins from Human Brain Tissue
11:49

Quantitative Proteomics Workflow using Multiple Reaction Monitoring Based Detection of Proteins from Human Brain Tissue

Published on: August 28, 2021

4.5K

Related Experiment Videos

Last Updated: Jul 12, 2025

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

9.5K
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

12.0K
Quantitative Proteomics Workflow using Multiple Reaction Monitoring Based Detection of Proteins from Human Brain Tissue
11:49

Quantitative Proteomics Workflow using Multiple Reaction Monitoring Based Detection of Proteins from Human Brain Tissue

Published on: August 28, 2021

4.5K

Area of Science:

  • Analytical Chemistry
  • Spectrometry
  • Biochemistry

Background:

  • Two-dimensional mass spectrometry (2D MS) is a powerful technique for analyzing complex samples.
  • Traditional 2D MS on FT-ICR MS relies on ion modulation for correlating precursor and fragment ions.
  • Ion isolation is typically required, limiting multiplexing capabilities.

Purpose of the Study:

  • To introduce quadrupolar detection for 2D MS within a dynamically harmonized ICR cell.
  • To explore the advantages of quadrupolar detection in enhancing 2D MS capabilities.
  • To develop and apply novel workflows for biomolecule analysis and quantification using this new method.

Main Methods:

  • Implementation of 2D MS with quadrupolar detection in a harmonized ICR cell.
  • Adaptation of data processing techniques for accurate frequency-to-mass conversion.
  • Application to top-down analysis of covalently labeled ubiquitin using ECD fragmentation.

Main Results:

  • Successful demonstration of 2D MS with quadrupolar detection in a harmonized ICR cell.
  • Established advantages of quadrupolar detection for comprehensive fragmentation analysis.
  • Developed a workflow for label-free relative quantification of biomolecule isoforms.

Conclusions:

  • Quadrupolar detection significantly enhances 2D MS capabilities by eliminating the need for ion isolation.
  • This method provides a robust platform for detailed biomolecule characterization.
  • The developed workflow facilitates label-free quantification of biomolecule isoforms, advancing proteomic studies.