Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

MALDI-TOF Mass Spectrometry

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...

Electrospray Ionization (ESI) Mass Spectrometry

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...

Matrix-Assisted Laser Desorption Ionization (MALDI)

Matrix-Assisted Laser Desorption Ionization (MALDI)

Matrix-assisted laser desorption ionization (MALDI) is a powerful analytical technique used in mass spectrometry. It enables the identification and characterization of various biomolecules, including proteins, peptides, nucleic acids, and carbohydrates. MALDI is an ionization technique, widely employed in biological and medical research, as well as in fields like pharmacology and biochemistry.The analyte of interest, a biomolecule or a mixture of biomolecules, is mixed with a suitable matrix...

Mass Spectrometry: Overview

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...

Chemical Ionization (CI) Mass Spectrometry

Chemical Ionization (CI) Mass Spectrometry

The molecular ion peak of a molecule in the mass spectrum provides vital information for molecular identification. However, conventional electron impact ionization can lead to the rapid dissociation of some molecular ions before they reach the detector. A milder ionization method is required to increase the lifetime of such ionized analyte molecules. Chemical ionization (CI) is a gas-phase protonation reaction useful for mass-analyzing analyte molecules that are easily protonated to yield the...

Mass Spectrometry: Complex Analysis

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...

You might also read

Related Articles

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

Sort by

Same author

Quantitation of Diastereomer Content in PS-Modified Synthetic Oligonucleotides using cIMS-MS.

Analytical chemistry·2026

Same author

Mapping GlycoRNAs on an Exosomal Surface.

Journal of the American Chemical Society·2026

Same author

Overexpression of GM3 and Ganglioside Pattern Remodeling in Lung Adenocarcinoma Brain Metastases Identified by Ion Mobility Mass Spectrometry.

International journal of molecular sciences·2025

Same author

Deficiency of Toll-like receptor 2 is a driver of sex-related compositional and structural rearrangements of membrane lipids.

Communications chemistry·2025

Same author

Advanced Ganglioside Characterization in Epileptic Human Hippocampus by Travelling Waves Ion Mobility Tandem Mass Spectrometry.

Journal of mass spectrometry : JMS·2025

Same author

Coupling Drift Tube Ion Mobility Measurements with Charge Detection Mass Spectrometry for the Analysis of Virus-like Particles and Other Megadalton-Sized Ions.

Analytical chemistry·2025

Search research articles

Related Experiment Video

Updated: Jun 10, 2026

Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments

Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments

Published on: January 20, 2022

Biomolecule analysis by ion mobility spectrometry.

Brian C Bohrer¹, Samuel I Merenbloom, Stormy L Koeniger

¹Department of Chemistry, Indiana University, Bloomington, 47405, USA. bbohrer@indiana.edu

Annual Review of Analytical Chemistry (Palo Alto, Calif.)

|July 20, 2010

Summary

Nonnative protein conformations, stable in the gas phase, can be separated using ion mobility spectrometry. This technique leverages differences in structure and mobility for complex biomolecule mixture analysis.

More Related Videos

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

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

Published on: July 31, 2010

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

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

Related Experiment Videos

Last Updated: Jun 10, 2026

Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments

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

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

Published on: July 31, 2010

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

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

Area of Science:

Biochemistry
Analytical Chemistry
Physical Chemistry

Background:

Nonnative protein conformations are typically unstable in solution but can be isolated in the gas phase.
Macromolecular ions generated via electrospray ionization exist in various charge states in the gas phase.
Structural differences in gas-phase conformations allow for separation based on mobility.

Purpose of the Study:

To review the differences between gas-phase and solution-phase nonnative protein states.
To explore the potential of ion mobility spectrometry for biomolecule separation.
To discuss the manipulation of gas-phase protein structures for enhanced analysis.

Main Methods:

Utilizing electrospray ionization to generate macromolecular ions.
Separating ions based on their differential mobilities in the gas phase.
Employing gentle collisional activation to induce structural transformations and alter mobilities.

Main Results:

Gas-phase nonnative protein conformations exhibit significant structural diversity.
Differences in ion mobility enable the separation of various shapes and charge states.
Collisional activation can induce new structures with distinct mobilities.

Conclusions:

Ion mobility spectrometry offers a pathway for multidimensional separation of biomolecules.
This technique can exploit structural differences of multiple stable states.
Ion mobility spectrometry is a promising rapid and sensitive method for complex mixture analysis prior to mass spectrometry.