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Related Concept Videos

Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

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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...
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Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

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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...
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Mass Spectrometry of Amines01:15

Mass Spectrometry of Amines

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In mass spectroscopy, amines undergo fragmentation to give parent ions with odd molecule weights. This observed mass spectrum follows the nitrogen rule; a molecule with an odd number of nitrogen atoms produces a molecular ion with an odd molecular weight. Amines undergo fragmentation through α cleavage, producing nitrogen-containing cations—iminium ions—and alkyl radicals. Mass spectra of aromatic and cyclic aliphatic amines exhibit strong molecular ion peaks, but acyclic...
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Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

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Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...
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Chemical Ionization (CI) Mass Spectrometry01:21

Chemical Ionization (CI) Mass Spectrometry

1.6K
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...
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Mass Spectrometry: Alkene Fragmentation00:59

Mass Spectrometry: Alkene Fragmentation

3.7K
Alkenes lose one electron from the unsaturated π bond upon ionization and form stable molecular ions. Further fragmentation of alkenes occurs through three different reaction pathways. The most prominent fragmentation is the cleavage at the allylic position. The resultant allylic carbocation is resonance stabilized. In the mass spectra of terminal alkenes, this fragment appears at a mass-to-charge ratio of 41. In the internal alkenes, where there are two choices of allylic cleavage, the...
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Related Experiment Video

Updated: Feb 16, 2026

Semi-Quantitative Analysis of Peptidoglycan by Liquid Chromatography Mass Spectrometry and Bioinformatics
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Mass spectrometry beyond the native state.

Shane A Chandler1, Justin Lp Benesch1

  • 1Department of Chemistry, Physical & Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UK.

Current Opinion in Chemical Biology
|December 31, 2017
PubMed
Summary
This summary is machine-generated.

Native mass spectrometry analyzes protein interactions in solution using vacuum-based methods. Recent advancements enhance its capability for detailed structural interrogation of proteins and their assemblies.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Mass Spectrometry

Background:

  • Native mass spectrometry (MS) probes protein interactions in solution under vacuum.
  • It offers high-resolution separation and high mass accuracy for analyzing multiple protein components.
  • Basic native MS determines the mass of intact proteins and their assemblies.

Purpose of the Study:

  • To describe recent developments in mass spectrometry approaches.
  • To explore structural interrogation of proteins in and beyond their native state.
  • To highlight advanced characterization opportunities enabled by ion motion control.

Main Methods:

  • Utilizing native mass spectrometry techniques.
  • Leveraging high-resolution separation and high mass accuracy.
  • Employing controlled ion motion in vacuum for detailed analysis.

Main Results:

  • Demonstrated advanced characterization of proteins and their assemblies.
  • Showcased extended opportunities beyond basic mass determination.
  • Highlighted recent developments in MS approaches for structural biology.

Conclusions:

  • Native mass spectrometry is a powerful tool for studying protein structures and interactions.
  • Recent advancements significantly expand its capabilities for detailed structural interrogation.
  • The technique provides deep insights into protein behavior in various states.