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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 electrospray 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...
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Peptide Identification Using Tandem Mass Spectrometry01:33

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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...
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MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

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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.
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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.
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Mass Spectrum: Interpretation01:24

Mass Spectrum: Interpretation

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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 low-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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Mass Spectrometry: Amine Fragmentation00:55

Mass Spectrometry: Amine Fragmentation

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Amines can be identified using mass spectroscopy based on their characteristic fragmentation patterns. The molecular ions of amines undergo fragmentation via ⍺-cleavage. The ⍺-cleavage of the carbon-carbon bonds in amines generates an alkyl radical and resonance-stabilized nitrogen-containing cation.
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Updated: Aug 1, 2025

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

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Studying protein structure and function by native separation-mass spectrometry.

Guusje van Schaick1, Rob Haselberg2, Govert W Somsen2

  • 1Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, Netherlands.

Nature Reviews. Chemistry
|April 28, 2023
PubMed
Summary
This summary is machine-generated.

Characterizing protein structure and function is vital. Coupling native protein separations with mass spectrometry offers a powerful, fast method for reliable analysis, aiding biomedical research.

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

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Last Updated: Aug 1, 2025

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

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Analyzing Large Protein Complexes by Structural Mass Spectrometry
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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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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
  • Proteomics

Background:

  • Protein structure alterations significantly impact biological function.
  • Understanding higher-order protein structure and structure-function relationships is critical.
  • Advanced analytical techniques are needed to characterize proteins in their native state.

Purpose of the Study:

  • To review native protein separation techniques.
  • To discuss practical aspects of hyphenating these separations with mass spectrometry.
  • To highlight affinity-based separations for simultaneous structural and functional protein information.

Main Methods:

  • Review of native separation modes for proteins.
  • Discussion of hyphenation strategies with mass spectrometry.
  • Emphasis on affinity-based separation techniques.

Main Results:

  • Native protein separations coupled with mass spectrometry provide a reliable, fast, and straightforward approach.
  • Affinity-based separations enable simultaneous acquisition of structural and functional protein data.
  • The reviewed methods have significant applications in biomedical and biopharmaceutical research.

Conclusions:

  • Native protein separation coupled with mass spectrometry is a rapidly emerging, powerful analytical strategy.
  • This approach is essential for studying protein structure-function relationships and conformational changes.
  • The techniques discussed offer valuable insights for biomedical and biopharmaceutical applications.