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Related Concept Videos

Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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Mass Spectrometry: Overview01:19

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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 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.
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Proteomics01:33

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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.
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Mass Spectrometry: Complex Analysis01:21

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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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Tandem Mass Spectrometry01:21

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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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Related Experiment Video

Updated: May 1, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
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Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 20, 2010

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Analysis of protein complexes using mass spectrometry.

Anne-Claude Gingras1, Matthias Gstaiger, Brian Raught

  • 1Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Ave, Room 992A, Toronto, Ontario, M5G 1X5, Canada. gingras@mshri.on.ca

Nature Reviews. Molecular Cell Biology
|June 28, 2007
PubMed
Summary

Affinity purification coupled with mass spectrometry (AP-MS) is a powerful tool for studying protein complexes and their interactions. Combining AP-MS with other methods enhances understanding of protein organization and assembly dynamics.

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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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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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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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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Protein complexes play crucial roles in cellular processes.
  • Understanding the composition and dynamics of protein complexes is essential for deciphering biological functions.
  • Affinity purification coupled with mass spectrometry (AP-MS) has emerged as a key technique in this field.

Purpose of the Study:

  • To highlight the versatility and applications of AP-MS in characterizing protein complexes.
  • To demonstrate how AP-MS can be integrated with other techniques for deeper insights.
  • To showcase the utility of AP-MS in studying protein-interaction networks and assembly dynamics.

Main Methods:

  • Affinity purification coupled with mass spectrometry (AP-MS).
  • Integration of AP-MS with biochemical fractionation.
  • Combination with intact mass measurement and chemical crosslinking.
  • Application of quantitative proteomics approaches alongside AP-MS.

Main Results:

  • AP-MS enables detailed characterization of protein complexes.
  • Integration with other methods aids in deciphering supramolecular organization.
  • Quantitative proteomics combined with AP-MS provides insights into assembly dynamics.

Conclusions:

  • AP-MS is a versatile and powerful technique for protein complex analysis.
  • Multi-technique approaches enhance the comprehensive understanding of protein organization and dynamics.
  • AP-MS is instrumental in mapping protein-interaction networks.