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

523
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...
523
High-Resolution Mass Spectrometry (HRMS)01:15

High-Resolution Mass Spectrometry (HRMS)

1.1K
The resolution of a mass spectrometer depends on the efficiency of separating ions with different ion masses. The mass of an atom is approximated to the sum of the masses of protons and neutrons inside, considering the masses of protons and neutrons as equal. However, the masses of the proton (1.6726 × 10−24 g) and neutron (1.6749 × 10−24 g) are not truly equal. There is a minor error in the expression of atomic masses relative to the simplest atom of hydrogen. For...
1.1K
Electrospray Ionization (ESI) Mass Spectrometry01:12

Electrospray Ionization (ESI) Mass Spectrometry

665
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...
665
Capillary Electrophoresis: Applications01:30

Capillary Electrophoresis: Applications

296
Capillary electrophoretic separations offer various modes, each with unique applications. These modes include capillary zone electrophoresis, capillary gel electrophoresis, capillary array electrophoresis, capillary isoelectric focusing, capillary isotachophoresis, micellar electrokinetic chromatography, and capillary electrochromatography.
Capillary zone electrophoresis (CZE) separates ionic components based on their electrophoretic mobility. It has been used to separate proteins, amino acids,...
296
Capillary Electrophoresis: Instrumentation01:20

Capillary Electrophoresis: Instrumentation

150
Capillary electrophoresis instrumentation typically consists of several key components. A high-voltage power supply generates the electric field necessary for the separation by connecting to an anode (the positively charged electrode) and a cathode (the negatively charged electrode) located in buffer reservoirs at each end of the capillary tube. The system includes a sample vial, a fused silica capillary tube coated with polyimide for mechanical strength through which the sample components...
150
Electrophoresis: Overview01:20

Electrophoresis: Overview

570
Electrophoresis is a powerful analytical separation technique that relies on the differential migration of charged species when subjected to an electric field. The core strength of electrophoresis lies in its ability to separate high-molecular-weight species in complex mixtures. It has found widespread use in biochemistry, molecular biology, and analytical chemistry, allowing the separation of compounds like amino acids, nucleotides, carbohydrates, and proteins with excellent resolution.
There...
570

You might also read

Related Articles

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

Sort by
Same author

Structure-guided design of broad-spectrum inhibitors of coronaviral proteases embodying a 1,3,2-oxazaphospholidin-3-one scaffold as a versatile design element.

European journal of medicinal chemistry·2026
Same author

Optimized Low-Field Differential Ion Mobility Separations with High-Resolution Mass Spectrometry for Top-Down Proteomics.

Analytical chemistry·2026
Same author

Macromolecular Separations by Ion Mobility Focusing in Divergent Asymmetric Electric Fields.

Analytical chemistry·2025
Same author

Improving the Quadrupole to Ion Mobility Region in a Digital Quadrupole/Ion Mobility/Orbitrap Mass Spectrometer.

Journal of the American Society for Mass Spectrometry·2025
Same author

Metal Polycation Adduction to Lipids Enables Superior Ion Mobility Separations with Ultrafast Ozone-Induced Dissociation.

Analytical chemistry·2024
Same author

Experimental Evaluation of Higher Order Stability Zones Using a Digitally Operated Quadrupole Mass Filter.

Journal of the American Society for Mass Spectrometry·2024
Same journal

Strain-Level Food Surveillance of <i>Escherichia coli</i> Using a Specific-Nonspecific Hybrid Sensor Array Strategy.

Analytical chemistry·2026
Same journal

A Field-Portable Fe(IV)-Mediated Competitive Quenching Chemiluminescence Platform with a Synchronous Y-Shaped Flow-through Cell for Broad-Spectrum Quantification of Volatile Phenols.

Analytical chemistry·2026
Same journal

Single-Molecule Characterization of CRISPR-Cas12a for Amplification-Free Genetic Testing.

Analytical chemistry·2026
Same journal

Integrated Acoustofluidic Manipulation and Oscillation-Stabilized Magnetic Relaxation Biosensing for <i>Salmonella</i> Detection.

Analytical chemistry·2026
Same journal

A Self-Powered Sensing Platform Based on the Janus Heterostructure for Machine Learning-Assisted Dual-Mode Detection of 17β-Estradiol.

Analytical chemistry·2026
Same journal

Large Language Model-Generated Dietary Metabolite Biomarker Database Drives Deep Annotation of the Human Diet Metabolome.

Analytical chemistry·2026
See all related articles

Related Experiment Video

Updated: May 13, 2025

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

4.2K

Superior Differential Ion Mobility Spectrometry of Pendular Macromolecules Using Low-Frequency Rectangular Waveforms.

Hayden A Thurman1, Egor Gusachenko1, Gordon A Anderson2

  • 1Department of Chemistry, Wichita State University, 1845 Fairmount, Wichita, Kansas 67260, United States.

Analytical Chemistry
|April 14, 2025
PubMed
Summary
This summary is machine-generated.

A new low-field differential ion mobility spectrometry (IMS) method enhances structural biology by measuring ion orientation. This technique overcomes limitations of traditional methods, offering improved resolution and accuracy for large molecules like proteins.

More Related Videos

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

24.5K
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

514

Related Experiment Videos

Last Updated: May 13, 2025

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

4.2K
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

24.5K
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

514

Area of Science:

  • Analytical Chemistry
  • Structural Biology
  • Physical Chemistry

Background:

  • Ion mobility spectrometry (IMS) is crucial for analyzing gas-phase ions and their geometries, aiding structural biology by revealing macromolecular folding and subunit connectivity.
  • Traditional IMS methods like linear and field asymmetric waveform IMS (FAIMS) suffer from orientational averaging, limiting resolution and structural specificity due to ion-molecule collision cross sections (Ω).
  • Existing FAIMS techniques utilize bisinusoidal waveforms, which can compromise measurement accuracy and correlation to ion properties, particularly for large biomolecules.

Purpose of the Study:

  • To introduce and evaluate a novel low-field differential (LOD) IMS technique for enhanced structural analysis of gas-phase ions.
  • To overcome the limitations of orientational averaging and waveform compromises inherent in existing IMS methods.
  • To enable the quantification of directional Ω (Ω⊥) for large ions by aligning macrodipoles in a low electric field.

Main Methods:

  • Development of a low-field differential (LOD) IMS stage operating at fields too weak for ion heating, enabling macrodipole alignment.
  • Utilizing rectangular waveforms with flexible frequency and duty cycle generated by direct switching, suitable for large ions with low mobility.
  • Experimental evaluation using the 66 kDa protein albumin, comparing results with previous bisinusoidal waveform studies.

Main Results:

  • The LOD IMS method successfully aligns strong macrodipoles, capturing their magnitudes and directional Ω (Ω⊥) without significant orientational averaging.
  • Rectangular waveforms generated in the new IMS stage offer improved resolution, measurement accuracy, and correlation to ion properties compared to bisinusoidal waveforms.
  • The technique demonstrated the quantification of Ω⊥ values for albumin by varying the duty cycle, showcasing its potential for large biomolecule analysis.

Conclusions:

  • Low-field differential IMS provides a significant advancement for structural biology by enabling the measurement of directional ion properties.
  • The developed LOD IMS system, with its flexible waveform generation and low-power format, offers a promising platform for detailed structural characterization.
  • This method enhances the structural specificity and resolution achievable with IMS, particularly for large and complex biomolecules.