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...
Ion-Exchange Chromatography01:09

Ion-Exchange Chromatography

Ion-exchange chromatography, or IEC, is a technique for separating ions based on their affinity for the stationary phase. The stationary phase is a cross-linked polymer resin with covalently attached ionic functional groups. The functional groups can be either positively charged (cation exchangers) or negatively charged (anion exchangers). A cation exchanger consists of a polymeric anion and active cations, while an anion exchanger is a polymeric cation with active anions. The choice 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...
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 Analyzers: Overview01:13

Mass Analyzers: Overview

The mass analyzer is a crucial component of the mass spectrometer. In the ionization chamber, the vaporized sample is bombarded with a high-energy electron beam to generate a radical cation and further fragment into neutral molecules, radicals, and cations. A series of negatively charged accelerator plates accelerate the cations into the mass analyzer. The mass analyzer separates ions according to their mass-to-charge (m/z) ratios and then directs them to the detector. The common types of mass...
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...

You might also read

Related Articles

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

Sort by
Same author

Complete enzyme clustering enhances coenzyme Q biosynthesis via substrate channeling.

Nature communications·2026
Same author

Investigating the relationship between ATP synthase and the TCA cycle by crosslinking mass spectrometry.

Nature communications·2026
Same author

Single-Ion Imaging Native Mass Spectrometry: Unraveling the Structural Features and Dissociation Energetics of Macromolecular Assemblies.

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

Immunoglobulin sub-class levels define inter-donor plasma variability: a longitudinal dual-lab study.

Molecular systems biology·2026
Same author

Foamy microglia link oxylipins to disease progression in multiple sclerosis.

Nature neuroscience·2026
Same author

Extending Serum IgG1 Antibody Repertoire Coverage Using DIA-PTCR.

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

Heterojunction-Enhanced Interfacial Evanescent-Tunable Fiber Optic Probe for Amplification-free CRISPR/Cas12a-Based Rapid and Ultrasensitive Detection of MPXV.

Analytical chemistry·2026
Same journal

Tunable Charge Transfer in Europium Metal-Organic Frameworks for Ratiometric Sensing of a Sarin Simulant.

Analytical chemistry·2026
Same journal

A β-Cyclodextrin/Ag<sub>2</sub>O@MWCNT-Based Stochastic Platform for the Simultaneous Molecular Enantiorecognition and Enantioanalysis of Twelve Amino Acids in Biological Matrices.

Analytical chemistry·2026
Same journal

The ACS at 150: The History of Analytical Chemistry Publications and a Century of Progress.

Analytical chemistry·2026
Same journal

Machine Learning-Enabled Image Analysis of Complex Chemical Mixtures: Synthetic Urine Droplets as a Test System.

Analytical chemistry·2026
Same journal

H<sub>2</sub>O<sub>2</sub>/Viscosity Tandem-Locked Fluorescent Probes Based on an In Situ Fluorophore Synthesis Strategy for Colitis Imaging and Diagnosis.

Analytical chemistry·2026
See all related articles

Related Experiment Video

Updated: May 13, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Analyses of Individual Singly Charged Ions Using a High-Field Orbitrap Analyzer.

Elena Giaretta1, Evolène Deslignière1,2, Eduard H T M Ebberink1

  • 1Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht 3584 CH, The Netherlands.

Analytical Chemistry
|May 12, 2026
PubMed
Summary
This summary is machine-generated.

High-field Orbitrap mass spectrometry now detects single-charge biomolecules. This advancement in charge detection mass spectrometry (CDMS) enhances resolution and sensitivity, expanding the capabilities for analyzing small molecules.

More Related Videos

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry
05:52

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry

Published on: January 12, 2024

Related Experiment Videos

Last Updated: May 13, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry
05:52

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry

Published on: January 12, 2024

Area of Science:

  • Analytical Chemistry
  • Mass Spectrometry
  • Biophysics

Background:

  • Orbitrap-based charge detection mass spectrometry (CDMS) analyzes biomolecules at the individual-ion level.
  • Longer transient recordings improve resolution and sensitivity in CDMS.
  • Singly charged analytes (1-2 kDa) were previously undetectable due to low signal-to-noise ratios (S/N).

Purpose of the Study:

  • To overcome the limitations of standard Orbitrap CDMS for singly charged analytes.
  • To implement and evaluate CDMS on a high-field Orbitrap (HF-OT) mass analyzer for extended mass-to-charge (m/z) ranges.
  • To establish new lower mass and charge limits for Orbitrap-based CDMS.

Main Methods:

  • Utilized a high-field Orbitrap (HF-OT, Exploris 480) mass spectrometer coupled to an external data acquisition system.
  • Adapted the mass spectrometer for robust detection across an extended m/z range (1 kDa to 500 kDa).
  • Enabled transient recording up to 20 seconds to enhance signal detection.

Main Results:

  • The HF-OT analyzer demonstrated superior charge and mass accuracy compared to a standard Orbitrap (S-OT) for various systems (insulin, BSA, monoclonal antibody).
  • Achieved unprecedented mass resolution exceeding 3 million at m/z ~4250.
  • Successfully detected singly charged peptides (angiotensin I, bradykinin) above the noise threshold (S/N = 2) for the first time, establishing new lower mass and charge limits.

Conclusions:

  • The modified HF-OT analyzer significantly enhances resolution and S/N, enabling the detection of low-mass, low-charge biomolecules.
  • This advancement expands the applicability of Orbitrap-based CDMS to a wider range of analytes, including peptides.
  • The study sets a new benchmark for sensitivity and mass accuracy in individual-ion mass analysis.