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

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...

You might also read

Related Articles

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

Sort by
Same author

Rational engineering of facultative anaerobiosis enables commensal survival in the oxygenated gut.

bioRxiv : the preprint server for biology·2026
Same author

Correction to "Multi-Laboratory Assessment Reveals Variable Ion Species Profiles in Electrospray Ionization Mass Spectrometer".

Journal of the American Society for Mass Spectrometry·2026
Same author

A Polysorbate Structural Atlas Curated from Drift Tube Ion Mobility-Mass Spectrometry Measurements.

Analytical chemistry·2026
Same author

Metabolomic Profiling of Squid Chromatophores Reveals Differential Biochemical Fingerprints across Red, Yellow, and Brown Colors.

Journal of proteome research·2026
Same author

Dehydration promotes intracellular lipid synthesis and accumulation.

Nature communications·2026
Same author

Desorption Electrospray Ionization-Mass Spectrometry Imaging Provides Spatiochemical Information on Potential Biocontrol Agents against <i>Phytophthora capsici</i> Infection in Tomato Plants.

Journal of the American Society for Mass Spectrometry·2026
Same journal

Morphology Assessment Enabled by Room-Temperature Soft-Landing in Native MS.

International journal of mass spectrometry·2026
Same journal

Impact of Supercharging on Top-Down Characterization of Monoclonal Antibodies by Collision Induced Dissociation.

International journal of mass spectrometry·2026
Same journal

Influence of Acceleration Field and Inlet Temperature on Ion Yields of Small Molecules in Atmospheric Pressure MALDI.

International journal of mass spectrometry·2026
Same journal

Optimising the choice of normalisation method for use in machine-learning classification of human blood plasma ambient ionisation mass spectra.

International journal of mass spectrometry·2026
Same journal

Mass spectrometry structural analysis of intrinsically disordered phosphoproteins.

International journal of mass spectrometry·2026
Same journal

Evaluation of Cleavable Crosslinking for Characterization of Proteoform Structural Differences by Top-Down Mass Spectrometry.

International journal of mass spectrometry·2026
See all related articles

Related Experiment Video

Updated: May 28, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Multiplexed Analysis of Peptide Functionality Using Lanthanide-based Structural Shift Reagents.

Thomas J Kerr1, Randi L Gant-Branum, John A McLean

  • 1Department of Chemistry, Vanderbilt Institute for Chemical Biology, and Vanderbilt Institute for Integrative Biosystems Research and Education, Vanderbilt University, 7330 Stevenson Center, Nashville, TN 37235.

International Journal of Mass Spectrometry
|October 4, 2011
PubMed
Summary
This summary is machine-generated.

Lanthanide-based reagents offer new ways to understand protein structures and expression levels using ion mobility-mass spectrometry. This method provides detailed peptide sequence and site localization for confident analysis.

More Related Videos

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Related Experiment Videos

Last Updated: May 28, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Proteomics

Background:

  • Elucidating protein structure and expression is crucial in biological research.
  • Current methods for peptide analysis can be limited in scope and confidence.
  • There is a need for advanced techniques to improve proteomic profiling.

Purpose of the Study:

  • To introduce lanthanide-based ion mobility shift reagents for protein and peptide analysis.
  • To demonstrate the utility of these reagents in obtaining structural and quantitative information.
  • To enhance peptide identification and site localization in complex mixtures.

Main Methods:

  • Development and application of lanthanide-based ion mobility shift reagents.
  • Utilizing ion mobility-mass spectrometry (IM-MS) for analysis.
  • Employing data-dependent acquisition for peptide sequencing and site localization.

Main Results:

  • Significant shifts in IM-MS conformation space due to high lanthanide mass.
  • Obtained sequence information and site localization for primary amines, phosphorylation sites, and cysteines.
  • Demonstrated confident peptide identification from complex samples.
  • Showcased potential for relative quantitation using stable lanthanide isotopes.

Conclusions:

  • Lanthanide-based IM-MS shift reagents are effective for protein structure elucidation.
  • The method enhances confidence in peptide identification and site localization.
  • Stable isotopes of lanthanides offer a viable approach for relative protein quantitation.