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...

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...

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...

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...

You might also read

Related Articles

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

Sort by

Same author

Untargeted Metabolomics Identifies Faecal Filtrate-Derived Metabolites That Disrupt <i>Clostridioides difficile</i> Metabolism and Confer Gut Barrier Cytoprotection.

International journal of molecular sciences·2025

Same author

Untargeted Metabolomic Characterization of Glioblastoma Intra-Tumor Heterogeneity Using OrbiSIMS.

Analytical chemistry·2023

Same author

Probing Interkingdom Signaling Molecules via Liquid Extraction Surface Analysis-Mass Spectrometry.

Analytical chemistry·2023

Same author

Metabolic alterations in dairy cattle with lameness revealed by untargeted metabolomics of dried milk spots using direct infusion-tandem mass spectrometry and the triangulation of multiple machine learning models.

The Analyst·2022

Same author

Time resolved growth of (N)-polycyclic aromatic hydrocarbons in engine deposits uncovered with OrbiSIMS depth profiling.

The Analyst·2022

Same author

Comprehensive LESA Mass Spectrometry Imaging of Intact Proteins by Integration of Cylindrical FAIMS.

Analytical chemistry·2020

Search research articles

Related Experiment Video

Updated: Aug 11, 2025

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Surface-sampling mass spectrometry to study proteins and protein complexes.

Kei F Carver Wong¹, Rebecca E Greatorex¹, Charlotte E Gidman¹

¹School of Pharmacy, University of Nottingham, Nottingham NG7 2RD, U.K.

Essays in Biochemistry

|February 7, 2023

Summary

This review covers surface mass spectrometry (MS) methods for intact protein and non-covalent complex analysis. It details matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) techniques, discussing their strengths and weaknesses.

Keywords:

imaging techniques mass spectrometry proteomics surface analysis

More Related Videos

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 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 11, 2025

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

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 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:

Analytical Chemistry
Biochemistry
Mass Spectrometry

Background:

Intact protein analysis and characterization of non-covalent complexes are crucial in proteomics and structural biology.
Traditional methods often involve protein denaturation or fragmentation, limiting structural insights.
Surface mass spectrometry offers a promising avenue for analyzing proteins in their native states.

Approach:

This review summarizes current surface mass spectrometry (MS) capabilities for intact protein and non-covalent complex analysis.
It discusses matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) based surface sampling techniques.
The review evaluates protein coverage, top-down elucidation, and structural probing for each method.

Key Points:

MALDI and ESI are primary surface MS techniques for intact protein analysis.
ESI-based surface sampling methods are explored for native protein and complex analysis.
Strategies for enhancing protein analysis include improved sample preparation, sampling, instrumentation, and ion mobility separation.

Conclusions:

Surface MS techniques provide valuable insights into intact protein structure and non-covalent interactions.
Each approach has distinct advantages and limitations that need consideration for specific applications.
Further advancements in sample handling, MS instrumentation, and separation techniques will expand the utility of surface MS for complex biological systems.