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Related Concept Videos

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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Related Experiment Video

Updated: May 22, 2026

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)
09:24

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)

Published on: December 18, 2020

Highly multiplexed targeted proteomics using precise control of peptide retention time.

Sebastien Gallien1, Scott Peterman, Reiko Kiyonami

  • 1Luxembourg Clinical Proteomics center (LCP), Centre de Recherche Public de la Santé, Strassen, Luxembourg.

Proteomics
|May 12, 2012
PubMed
Summary

This study introduces dynamic retention time correction for large-scale proteomics. This method enhances the robustness and automation of targeted assays, improving sensitivity and selectivity in LC-MS/MS experiments.

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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

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Last Updated: May 22, 2026

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)
09:24

Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)

Published on: December 18, 2020

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Mass Spectrometry

Background:

  • Large-scale proteomics using Selected Reaction Monitoring (SRM) on triple quadrupole mass spectrometers faces challenges in experimental design.
  • Increased numbers of targeted peptides can negatively impact the sensitivity and selectivity balance in LC-MS/MS methods.
  • Time-scheduled SRM transition acquisition is employed to manage large target numbers.

Purpose of the Study:

  • To extend the application of peptide trainer kits for building SRM methods.
  • To enable real-time elution profile characterization for automated adjustment of scheduled detection windows.
  • To improve the robustness of targeted discovery and routine quantification experiments.

Main Methods:

  • Utilizing well-characterized synthetic peptides for chromatographic characterization of elution profiles.
  • Implementing dynamic retention time adjustments for automated correction of LC variations.
  • Developing a dynamic retention correction approach to identify and correct common LC variations.

Main Results:

  • Demonstrated successful characterization of elution profiles for most endogenous peptides using peptide trainer kits.
  • Enabled automated adjustment of scheduled detection windows through real-time elution profile characterization.
  • Significantly improved the robustness of targeted assays, allowing for multi-day experiments without constant supervision.

Conclusions:

  • Dynamic retention correction enhances the reliability of large-scale targeted proteomics.
  • Automated adjustment of scheduled detection windows improves assay efficiency and reduces manual intervention.
  • This approach offers a robust solution for both targeted discovery and routine quantification in proteomics.