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

Mass Spectrometers01:16

Mass Spectrometers

This lesson details the instrumentation of a mass spectrometer—a physical instrument to perform mass spectrometry on analyte molecules and record the characteristic mass spectra. This is achieved via three chief functions:
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 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...
Mass Analyzers: Common Types01:19

Mass Analyzers: Common Types

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...
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...
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...

You might also read

Related Articles

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

Sort by
Same author

Self-regulated learning and academic success in health professions students: A systematic review.

Medical teacher·2026
Same author

Mass spectrometry-based mapping of conformational epitopes on SARS-CoV-2 antigens targeted by monoclonal antibodies.

International journal of biological macromolecules·2026
Same author

Do interactions between different Selfish Genetic Elements matter?

Journal of evolutionary biology·2026
Same author

Drug Burden Index and Its Association With Functional Outcomes in Patients Receiving Hemodialysis.

Kidney medicine·2026
Same author

Who Should Decide the Outcome for a Clinical Trial? Comparing the Views of Stakeholders on Intervention Benefit Using Multi-Criteria Decision Modelling of Cognitive Remediation.

Schizophrenia bulletin·2026
Same author

Non-invasive detection of salivary TNF-α enabled by hemp-derived nanocellulose nanocomposite electrochemical immunosensor for point-of-care diagnostics.

Bioelectrochemistry (Amsterdam, Netherlands)·2026

Related Experiment Video

Updated: Jul 17, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: August 1, 2010

Multiplexed MS/MS in a quadrupole ion trap mass spectrometer.

Jonathan Wilson1, Richard W Vachet

  • 1Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA.

Analytical Chemistry
|December 15, 2004
PubMed
Summary

A new multiplexing method enables simultaneous MS/MS analysis of multiple peptide ions in quadrupole ion trap mass spectrometry (QITMS). This approach enhances sample throughput and reduces analysis time by encoding ion intensity.

More Related Videos

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)
09:24

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)

Published on: December 18, 2020

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

Related Experiment Videos

Last Updated: Jul 17, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: August 1, 2010

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)
09:24

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)

Published on: December 18, 2020

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

Area of Science:

  • Analytical Chemistry
  • Mass Spectrometry
  • Biochemistry

Background:

  • Conventional tandem mass spectrometry (MS/MS) can be time-consuming for analyzing multiple samples.
  • Quadrupole ion trap mass spectrometers (QITMS) have specific ion accumulation characteristics.

Purpose of the Study:

  • To develop a multiplexing method for simultaneous MS/MS analysis of multiple peptide ions in QITMS.
  • To leverage QITMS ion accumulation properties for improved efficiency.

Main Methods:

  • Developed a multiplexing strategy utilizing inherent mass bias during ion accumulation in QITMS.
  • Employed Gaussian distributions relating ion intensity to RF trapping voltages for intensity encoding.
  • Utilized two arbitrary waveforms for ion isolation and dissociation.

Main Results:

  • Successfully correlated 66% of product ions from five precursor peptide ions using the multiplexing method.
  • Achieved accurate identification with only 6% misidentification of remaining product ions.
  • Demonstrated potential for increased sample throughput and reduced analysis times.

Conclusions:

  • The developed multiplexing method offers a significant advancement for MS/MS analysis in QITMS.
  • This technique can enhance efficiency, reduce analysis time, and improve signal-to-noise ratios.
  • The method shows promise for high-throughput proteomic studies.