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Related Concept Videos

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...
Mass Spectrometry: Overview01:19

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...
Mass Spectrometry: Complex Analysis01:21

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...
Chemical Ionization (CI) Mass Spectrometry01:21

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...
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 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...

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Updated: Jun 25, 2026

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
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Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

Using electrospray ionisation mass spectrometry to study non-covalent interactions.

Bryan J McCullough1, Simon J Gaskell

  • 1The Michael Barber Centre for Mass Spectrometry, The University of Manchester, Manchester Interdisciplinary Biocentre, The John Garside Building, 131 Princess Street, Manchester M17DN, UK.

Combinatorial Chemistry & High Throughput Screening
|February 10, 2009
PubMed
Summary

Electrospray ionization mass spectrometry is ideal for studying non-covalent interactions due to its soft nature and multiply charged ions. This review covers mass spectrometry methods for characterizing non-covalent protein complexes.

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

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Last Updated: Jun 25, 2026

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
09:18

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

Sample Preparation for Probe Electrospray Ionization Mass Spectrometry
05:47

Sample Preparation for Probe Electrospray Ionization Mass Spectrometry

Published on: February 19, 2020

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

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Mass Spectrometry

Background:

  • Electrospray ionization (ESI) is a key technique in mass spectrometry.
  • ESI's soft nature and ability to generate multiply charged ions are crucial.
  • These properties are ideal for investigating weak molecular interactions.

Purpose of the Study:

  • To review the fundamental principles of studying non-covalent interactions using mass spectrometry.
  • To highlight mass spectrometry-based methods for characterizing non-covalent protein complexes.
  • To provide examples from current research.

Main Methods:

  • Mass spectrometry
  • Electrospray ionization
  • Analysis of non-covalent protein complexes

Main Results:

  • ESI enables the study of transient, low-affinity biomolecular assemblies.
  • Mass spectrometry can provide information on stoichiometry, binding affinities, and dynamics.
  • Various MS-based approaches exist for characterizing these complexes.

Conclusions:

  • Mass spectrometry, particularly ESI-MS, is a powerful tool for non-covalent interaction analysis.
  • Continued development of MS techniques will further advance the understanding of protein complex behavior.
  • This review provides a foundation for researchers in the field.