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

Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

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...
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...
Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
Mass Spectrum: Interpretation01:24

Mass Spectrum: Interpretation

An unknown compound can be established by identifying the molecular ion peak in the mass spectrum. The molecular ion peak is often weak or absent due to the predominance of fragmentation in high-energy electron beams. In such cases, a soft-energy electron beam can be used to scan the spectrum to enhance the intensity of the molecular ion peak. Additionally, chemical ionization, field ionization, and desorption ionization spectra are used to obtain a relatively intense molecular ion peak.To...

You might also read

Related Articles

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

Sort by
Same author

Integrated Native Mass Spectrometry Imaging of Soluble and Membrane Proteins.

Journal of the American Chemical Society·2026
Same author

Imaging of Protein Assemblies up to 231 kDa in Tissues with Nano-DESI Mass Spectrometry.

Analytical chemistry·2025
Same author

Comparative Whole Genome Phylogeography Reveals Genetic Distinctiveness of Appalachian Populations of Boreal Songbirds.

Evolutionary applications·2025
Same author

Editorial: "2024 Emerging Investigators".

Journal of the American Society for Mass Spectrometry·2025
Same author

Native ambient mass spectrometry of membrane proteins directly from bacterial colonies.

Chemical communications (Cambridge, England)·2025
Same author

Infrared Photoactivation Enables nano-DESI MS of Protein Complexes in Tissue on a Linear Ion Trap Mass Spectrometer.

Journal of the American Society for Mass Spectrometry·2024
Same journal

Advances in application of microplasmas for non-metallic species analysis by optical spectrometry.

The Analyst·2026
Same journal

Sulfur vacancy-mediated self-photocatalysis-boosted electrochemiluminescence sensing <i>via</i> molecular oxygen activation for sensitive detection of isocarbophos.

The Analyst·2026
Same journal

Analytical challenges in mapping the subcellular metabolome and lipidome.

The Analyst·2026
Same journal

Threshold-guided multiplex PCR-LFA: a step toward UTI pathogen detection.

The Analyst·2026
Same journal

Aptamer-based CRISPR-Cas12a fluorescent biosensors for serum biomarker detection.

The Analyst·2026
Same journal

A two-step centrifugal microfluidic platform for semi-automated IGRA detection of tuberculosis based on chemiluminescence.

The Analyst·2026
See all related articles

Related Experiment Video

Updated: May 31, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Dissociation techniques in mass spectrometry-based proteomics.

Andrew W Jones1, Helen J Cooper

  • 1School of Biosciences, College of Life and Environmental Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.

The Analyst
|June 24, 2011
PubMed
Summary
This summary is machine-generated.

Proteomics uses mass spectrometry to analyze proteins. Key fragmentation techniques like collision-induced dissociation, electron capture dissociation, and electron transfer dissociation are explored for protein sequencing and modification analysis.

More Related Videos

Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools
07:01

Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools

Published on: August 19, 2025

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

Related Experiment Videos

Last Updated: May 31, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools
07:01

Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools

Published on: August 19, 2025

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

Background:

  • The field of proteomics has rapidly expanded.
  • Mass spectrometry is central to large-scale protein analysis.
  • Understanding protein sequence and modifications is crucial.

Purpose of the Study:

  • To describe fragmentation techniques in mass spectrometry-based proteomics.
  • To discuss principles, advantages, limitations, and applications of these techniques.
  • To highlight their role in protein identification and characterization.

Main Methods:

  • Collision-induced dissociation (CID)
  • Electron capture dissociation (ECD)
  • Electron transfer dissociation (ETD)

Main Results:

  • Detailed explanation of CID, ECD, and ETD principles.
  • Comparison of advantages and limitations for each technique.
  • Overview of their applications in proteomics research.

Conclusions:

  • Fragmentation techniques are essential for mass spectrometry-based proteomics.
  • CID, ECD, and ETD offer distinct capabilities for peptide and protein analysis.
  • These methods advance the understanding of protein structure and function.