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Related Concept Videos

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...
Proteomics01:33

Proteomics

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.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

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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Updated: May 21, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Mass spectrometry-based structural proteomics.

Jason J Serpa1, Carol E Parker, Eveniy V Petrotchenko

  • 1University of Victoria-Genome British Columbia Proteomics Centre, University of Victoria, Victoria, BC V8Z 7X8, Canada.

European Journal of Mass Spectrometry (Chichester, England)
|May 30, 2012
PubMed
Summary
This summary is machine-generated.

Structural proteomics uses mass spectrometry and protein chemistry to map protein structures and interactions. Combining methods like crosslinking and hydrogen/deuterium exchange provides comprehensive data for biological insights.

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Analyzing Large Protein Complexes by Structural Mass Spectrometry
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Proteomics

Background:

  • Structural proteomics integrates protein chemistry and mass spectrometry.
  • It addresses challenges in characterizing protein structures, assemblies, and interactions.
  • Understanding protein interactions is crucial in molecular biology and drug discovery.

Purpose of the Study:

  • To provide an overview of structural proteomics methodologies.
  • To illustrate the application of these techniques with examples.
  • To highlight the utility of combined approaches for biological questions.

Main Methods:

  • Crosslinking followed by mass spectrometry.
  • Photoaffinity labeling and chemical protein modification.
  • Limited proteolysis and hydrogen/deuterium exchange (HDX).

Main Results:

  • Individual methods offer incomplete structural information.
  • Complementary techniques combined yield comprehensive data.
  • Detailed interfaces of protein-protein and protein-ligand interactions can be elucidated.

Conclusions:

  • Structural proteomics is a powerful approach for detailed molecular characterization.
  • Combining multiple mass spectrometry-based techniques enhances structural determination.
  • This field offers critical insights into biological mechanisms and potential drug targets.