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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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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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Related Experiment Video

Updated: Mar 9, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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A General Method for Targeted Quantitative Cross-Linking Mass Spectrometry.

Juan D Chavez1, Jimmy K Eng1, Devin K Schweppe1

  • 1Department of Genome Sciences, University of Washington School of Medicine, Seattle, WA, United States of America.

Plos One
|December 21, 2016
PubMed
Summary
This summary is machine-generated.

Chemical cross-linking mass spectrometry (XL-MS) now offers a streamlined method for analyzing protein structures. This technique simplifies the measurement of dynamic protein changes and interactions using accessible LC-MS systems.

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Area of Science:

  • Structural Biology
  • Proteomics
  • Biochemistry

Background:

  • Chemical cross-linking mass spectrometry (XL-MS) reveals protein structure by identifying linked amino acid residues.
  • XL-MS data complements other structural biology techniques like X-ray crystallography, NMR, and cryo-electron microscopy.
  • Quantitative proteomics combined with XL-MS can offer insights into protein structural dynamics and complex formation.

Purpose of the Study:

  • To develop a general method for targeted quantitative mass spectrometric analysis of cross-linked peptide pairs.
  • To adapt the open-source software Skyline for analyzing quantitative XL-MS data, facilitating data sharing and method dissemination.
  • To demonstrate the robustness and utility of the developed method through a cross-laboratory study.

Main Methods:

  • Adaptation of the Skyline software package for the targeted quantitative analysis of cross-linked peptides.
  • Implementation of a general method for quantitative mass spectrometric analysis of cross-linked peptide pairs.
  • Validation of the method through a cross-laboratory study, comparing results with previously published data.

Main Results:

  • Successful adaptation of Skyline for quantitative XL-MS data analysis, enabling easier data interpretation and sharing.
  • Demonstration of the method's utility and robustness across different laboratories.
  • Validation of quantified cross-linked peptide pairs, confirming the accuracy and reliability of the approach.

Conclusions:

  • The developed method provides an accessible resource for quantitative XL-MS analysis.
  • Laboratories with LC-MS systems can now readily and accurately measure dynamic changes in protein structure and interactions.
  • This advance lowers the barrier for widespread adoption of quantitative XL-MS techniques in structural biology research.