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 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 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:
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...
Electrospray Ionization (ESI) Mass Spectrometry01:12

Electrospray Ionization (ESI) Mass Spectrometry

Higher molecular weight biomolecules are nonvolatile compounds that may decompose before ionizing or vaporizing during mass analysis with conventional electron impact ionization methods. Accordingly, electrospray ionization (ESI) is the favored method for vaporizing and ionizing biomolecules as it circumvents rapid fragmentation and enables the recording of mass signals for the entire biomolecule.
ESI utilizes electrical energy to transfer ions from the liquid phase of the sample into the...
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 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...

You might also read

Related Articles

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

Sort by
Same author

Translational bottlenecks in blood-based proteomics.

EMBO molecular medicine·2026
Same author

A comparison of deep multiomics profiles across ethnicity, geography, and age.

Cell·2026
Same author

Activation of Oligonucleotide Polyanions Using Collisions, Electrons and Photons in a timsOmni Platform.

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

Parallel Sequencing of the Two Arms on a Bispecific Antibody by Electron Capture Dissociation on a timsOmni Platform Reveals Several By-products in the Controlled Fab-arm Exchange Process.

Analytical chemistry·2026
Same author

A Prototype timsOmni Platform Enables Confident Annotation of the Key Hypervariable CDR3 Regions of IgG Immunoglobulins Using Low- and High-Energy Electron-Based Fragmentation.

Analytical chemistry·2026
Same author

Direct Observation of Metastable Fragment Ions in Ultraviolet Photodissociation of Ubiquitin.

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

Mass Spectrometry Insights Into Post-Translational Modifications in Extracellular Vesicles.

Mass spectrometry reviews·2026
Same journal

Standardization Challenges and Breakthroughs in Apolipoprotein B Detection: From Immunoassays to LC-MS/MS.

Mass spectrometry reviews·2026
Same journal

Carlito B. Lebrilla: Building Instruments, Fields and Opportunities From the Ground up.

Mass spectrometry reviews·2026
Same journal

Recent Advances in Top-Down Proteomics for Single-Cell Research.

Mass spectrometry reviews·2026
Same journal

Applications of Top-Down Protein Analysis in Clinical Diagnostics.

Mass spectrometry reviews·2026
Same journal

Recent Advances (2023-2025) of Capillary Electrophoresis-Mass Spectrometry (CE-MS) for Top-Down Proteomics.

Mass spectrometry reviews·2026
See all related articles

Related Experiment Video

Updated: Jun 18, 2026

Detection of Regulated Ergot Alkaloids in Food Matrices by Liquid Chromatography-Trapped Ion Mobility Spectrometry-Time-of-Flight Mass Spectrometry
08:56

Detection of Regulated Ergot Alkaloids in Food Matrices by Liquid Chromatography-Trapped Ion Mobility Spectrometry-Time-of-Flight Mass Spectrometry

Published on: November 22, 2024

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

Erin M Panczyk1, Claudia Martelli2, Mark E Ridgeway1

  • 1Bruker Scientific, LLC, Billerica, Massachusetts, USA.

Mass Spectrometry Reviews
|June 17, 2026
PubMed
Summary
This summary is machine-generated.

Trapped ion mobility spectrometry (TIMS) offers a versatile alternative for analyzing ions by electric fields, enhancing separation for omics sciences. This technology provides increased peak capacity and deeper peptide identification in mass spectrometry.

Keywords:
PASEFTIMSion mobility

More Related Videos

Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments
08:40

Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments

Published on: January 20, 2022

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: July 31, 2010

Related Experiment Videos

Last Updated: Jun 18, 2026

Detection of Regulated Ergot Alkaloids in Food Matrices by Liquid Chromatography-Trapped Ion Mobility Spectrometry-Time-of-Flight Mass Spectrometry
08:56

Detection of Regulated Ergot Alkaloids in Food Matrices by Liquid Chromatography-Trapped Ion Mobility Spectrometry-Time-of-Flight Mass Spectrometry

Published on: November 22, 2024

Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments
08:40

Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments

Published on: January 20, 2022

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: July 31, 2010

Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Structural Biology

Background:

  • Trapped ion mobility spectrometry (TIMS) is a versatile alternative to drift tube ion mobility spectrometry.
  • TIMS analyzes ions using an electric field, trapping them against a moving gas flow.
  • Its small size and low operating voltage facilitate hybridization with mass spectrometry.

Purpose of the Study:

  • To review different designs and operational modes of TIMS.
  • To highlight the advantages, potentials, and challenges of TIMS in omics sciences.
  • To introduce new TIMS platforms and discuss future applications.

Main Methods:

  • Ions are accumulated and trapped in an electric field.
  • Elution occurs based on collision cross section (CCS) as the electric field strength is scanned.
  • TIMS is coupled with Time-of-Flight Mass Spectrometry (TOFMS) for analysis.

Main Results:

  • TIMS-MS coupling enhances peak capacity, reducing mass spectra complexity.
  • This leads to a greater depth of peptide identification in bottom-up proteomics.
  • TIMS has found broad applications in proteomics, glycomics, metabolomics, lipidomics, and native mass spectrometry.

Conclusions:

  • TIMS technology offers significant advantages for various omics sciences, including metabolomics and structural biology.
  • Its integration with mass spectrometry, particularly the timsTOF instrument, has established it as a key analytical tool.
  • Future directions include advanced platforms for single-cell analysis and broader structural biology applications.