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...
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...

You might also read

Related Articles

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

Sort by
Same author

Use of Machine Learning to Identify Markers of Risk for Fragile X-Associated Tremor/Ataxia Syndrome: A Preliminary Analysis.

Annals of neurology·2026
Same author

Comprehensive, multidisciplinary care for fragile X-associated tremor/ataxia syndrome.

Frontiers in neurology·2026
Same author

<i>De novo</i> and quiescent cGVHD are distinguishable in a prognostic biomarker panel.

Frontiers in immunology·2026
Same author

T2-FLAIR hyperintensities in the inferior cerebellar peduncles and their association with clinical symptoms, molecular and MRI markers in male <i>FMR1</i> premutation carriers.

Frontiers in molecular neuroscience·2026
Same author

Association between specialized nutrition support and 90-day mortality relative to standard of care in malnourished adults with decompensated cirrhosis: A retrospective cohort study.

JPEN. Journal of parenteral and enteral nutrition·2026
Same author

Behavioral Phenotype Associations With Resting State EEG Signal Complexity and Power Spectral Density in Fragile X Syndrome.

Autism research : official journal of the International Society for Autism Research·2026

Related Experiment Video

Updated: Jun 1, 2026

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification
09:04

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Proton transfer reactions for improved peptide characterisation.

Marko Rožman1, Andrea Schneider, Simon J Gaskell

  • 1Laboratory for Chemical Kinetics and Atmospheric Chemistry, Ruđer Bošković Institute, Zagreb, Croatia. marko@irb.hr

Journal of Mass Spectrometry : JMS
|June 2, 2011
PubMed
Summary

Combining deprotonation with low-energy collision-induced dissociation (CID) enhances tryptic peptide characterization by analyzing multiple precursor charge states. This method improves data richness and identification confidence for peptides containing arginine or lysine.

More Related Videos

Sample Preparation and Relative Quantitation using Reductive Methylation of Amines for Peptidomics Studies
08:00

Sample Preparation and Relative Quantitation using Reductive Methylation of Amines for Peptidomics Studies

Published on: November 4, 2021

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
09:18

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

Related Experiment Videos

Last Updated: Jun 1, 2026

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification
09:04

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Sample Preparation and Relative Quantitation using Reductive Methylation of Amines for Peptidomics Studies
08:00

Sample Preparation and Relative Quantitation using Reductive Methylation of Amines for Peptidomics Studies

Published on: November 4, 2021

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
09:18

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

Area of Science:

  • Proteomics and Mass Spectrometry
  • Analytical Chemistry

Background:

  • Characterization of tryptic peptides is crucial for protein identification and functional analysis.
  • Traditional mass spectrometry methods often rely on single precursor charge states, potentially limiting structural information.
  • Collision-induced dissociation (CID) is a common fragmentation technique in mass spectrometry.

Purpose of the Study:

  • To explore the combination of deprotonation and low-energy CID for enhanced characterization of tryptic peptides.
  • To investigate the benefits of accessing multiple precursor charge states (singly and doubly protonated) in a single experiment.
  • To improve database identification confidence and distinguish between different types of tryptic peptides.

Main Methods:

  • Utilized ion/molecule and ion/ion reactions for deprotonation to generate singly and doubly protonated peptide precursors.
  • Applied low-energy collision-induced dissociation (CID) to these different charge states.
  • Analyzed fragmentation patterns and sequence ions from both singly and doubly charged precursors.

Main Results:

  • The combined approach provided instant access to fragmentation data from both singly and doubly protonated precursors.
  • Analysis of combined data sets (singly and doubly charged precursors) resulted in a ~37% increase in database identification confidence compared to single charge state analysis.
  • Distinct fragmentation patterns between singly and doubly charged precursors allowed for differentiation of arginine- or lysine-containing tryptic peptides.

Conclusions:

  • Combining deprotonation with low-energy CID offers a powerful strategy for enhanced peptide characterization.
  • Analyzing multiple precursor charge states significantly expands structurally informative data and improves identification confidence.
  • This method facilitates the distinction of specific peptide classes based on their fragmentation behavior.