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Related Concept Videos

Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

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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...
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Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

9.0K
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...
2.6K
Mass Spectrometry of Amines01:15

Mass Spectrometry of Amines

5.4K
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...
5.4K
Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

4.3K
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...
4.3K
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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Analyzing Large Protein Complexes by Structural Mass Spectrometry
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Analyzing Large Protein Complexes by Structural Mass Spectrometry

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Characterizing Intact Macromolecular Complexes Using Native Mass Spectrometry.

Elisabetta Boeri Erba1, Luca Signor2, Mizar F Oliva2

  • 1Institut de Biologie Structurale (IBS), Université de Grenoble Alpes, CEA, CNRS, Grenoble, France. elisabetta.boeri-erba@ibs.fr.

Methods in Molecular Biology (Clifton, N.J.)
|April 2, 2018
PubMed
Summary
This summary is machine-generated.

Native mass spectrometry (MS) offers sensitive characterization of macromolecular assemblies, revealing subunit stoichiometry and interaction networks. This workflow details native MS experiments and protein quality control using mass spectrometry in denaturing conditions.

Keywords:
Macromolecular assembliesNative mass spectrometryStoichiometryTwo-dimensional map of interactions

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

  • Biochemistry
  • Analytical Chemistry
  • Structural Biology

Background:

  • Macromolecular assemblies are crucial biological entities.
  • Understanding their structure and dynamics is essential for biological insights.
  • Native mass spectrometry (MS) is a powerful tool for analyzing these complexes.

Purpose of the Study:

  • To describe a workflow for performing native MS experiments.
  • To demonstrate the characterization of macromolecular assemblies using native MS.
  • To illustrate protein quality control analysis via MS under denaturing conditions.

Main Methods:

  • Native mass spectrometry (MS) for analyzing intact macromolecular complexes.
  • Denaturing mass spectrometry for protein quality control.
  • Detailed workflow description for native MS experiments.

Main Results:

  • Native MS provides high sensitivity for characterizing macromolecular assemblies.
  • The technique reveals subunit stoichiometry and 2D interaction networks.
  • Information on the dynamic behavior of macromolecular complexes can be obtained.
  • MS in denaturing conditions is effective for protein quality control.

Conclusions:

  • Native MS is a versatile technique for detailed structural and dynamic analysis of macromolecular assemblies.
  • The described workflow facilitates the application of native MS.
  • Mass spectrometry, in both native and denaturing conditions, is valuable for comprehensive protein analysis.