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

Peptide Identification Using Tandem Mass Spectrometry

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...

You might also read

Related Articles

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

Sort by

Same author

Orbitrap Collision Cross Section Measurements Enhance Isomer Annotations in Lipidomics.

bioRxiv : the preprint server for biology·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

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

Analytical chemistry·2026

Same author

Extending Serum IgG1 Antibody Repertoire Coverage Using DIA-PTCR.

Journal of the American Society for Mass Spectrometry·2026

Same author

First 20 Years of Orbitrap Mass Spectrometry as the Mainstream Analytical Technique.

Mass spectrometry reviews·2026

Same author

Higher-Throughput Proteome Profiling Enabled by Parallelized Pre-Accumulation and Optimized Ion Processing in the Orbitrap Astral Zoom Mass Spectrometer.

Molecular & cellular proteomics : MCP·2026

Search research articles

Related Experiment Video

Updated: Aug 30, 2025

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

A Preparative Mass Spectrometer to Deposit Intact Large Native Protein Complexes.

Paul Fremdling¹, Tim K Esser¹, Bodhisattwa Saha¹

¹Chemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.

|August 29, 2022

Summary

Electrospray ion-beam deposition (ES-IBD) is now accessible on a commercial mass spectrometry platform, enabling gentle molecule manipulation and gas-phase analysis. This innovation facilitates structural biology studies by preserving molecular integrity during deposition and analysis.

Keywords:

ES-IBD TEM energy width enzymatic activity native MS soft landing transmission

More Related Videos

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

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

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

Published on: October 15, 2018

Related Experiment Videos

Last Updated: Aug 30, 2025

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

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

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

Published on: October 15, 2018

Area of Science:

Molecular Biophysics
Analytical Chemistry
Structural Biology

Background:

Electrospray ion-beam deposition (ES-IBD) is a powerful technique for studying molecular structure and reactivity.
Current ES-IBD instruments are custom-built and not commercially available, limiting accessibility.
ES-IBD enables gentle gas-phase manipulation and deposition of molecules onto substrates for analysis.

Purpose of the Study:

To develop a module that integrates ES-IBD capabilities into a commercial mass spectrometry (MS) platform.
To assess the performance characteristics of the integrated ES-IBD system.
To demonstrate the utility of ES-IBD for structural biology applications.

Main Methods:

Integration of an ES-IBD module with a Thermo Scientific Q Exactive UHMR mass spectrometer.
Characterization of beam intensity, landing-energy control, and deposition spot size.
Analysis of deposited molecules using atomic force microscopy (AFM) and transmission electron microscopy (TEM).
Enzymatic activity assays on deposited noncovalent protein complexes.

Main Results:

The integrated system demonstrates controlled beam intensity, landing-energy, and deposition spot size for diverse molecules.
AFM and TEM imaging successfully distinguished near-native from unfolded proteins and preserved protein assembly shapes.
Enzymatic activity of a noncovalent complex was quantified after deposition.
The ES-IBD module offers a more accessible alternative to custom-built instruments.

Conclusions:

The developed module significantly enhances the accessibility of ES-IBD for structural biology research.
ES-IBD on a commercial platform preserves molecular structure and function after deposition.
Further optimization is needed to fully realize the potential of ES-IBD in structural biology.