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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

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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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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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Related Experiment Video

Updated: Mar 25, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
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Large-Scale and Deep Quantitative Proteome Profiling Using Isobaric Labeling Coupled with Two-Dimensional LC-MS/MS.

Marina A Gritsenko1, Zhe Xu1, Tao Liu2

  • 1Biological Sciences Division and Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA, 99352, USA.

Methods in Molecular Biology (Clifton, N.J.)
|February 13, 2016
PubMed
Summary
This summary is machine-generated.

This study presents a quantitative proteomic strategy using isobaric labeling and 2D-LC-MS/MS for deep profiling of proteins and posttranslational modifications (PTMs). This method enables comprehensive analysis of clinical samples like tumors for disease insights.

Keywords:
Isobaric labelingMass spectrometryQuantitative proteomicsTwo-dimensional liquid chromatographyiTRAQ

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Area of Science:

  • Proteomics
  • Mass Spectrometry
  • Biochemistry

Background:

  • Quantitative proteomic data on protein abundances and posttranslational modifications (PTMs) are crucial for understanding disease pathogenesis and developing therapies.
  • Current methods may lack the depth and scale required for comprehensive analysis of complex biological and clinical samples.

Purpose of the Study:

  • To introduce a novel quantitative strategy for large-scale, deep proteome profiling.
  • To enable integrated characterization of proteomes and PTMs in clinical specimens.
  • To facilitate comprehensive quantitative proteomic analysis across large patient cohorts.

Main Methods:

  • Utilized isobaric stable isotope-labeling techniques for multiplexed and accurate peptide quantification.
  • Employed two-dimensional liquid chromatography-tandem mass spectrometry (2D-LC-MS/MS) for deep proteome profiling.
  • Incorporated reversed-phase LC fractionation and nano-LC coupled to high-resolution MS for high-confidence identification and quantification.

Main Results:

  • Successfully applied the strategy for in-depth quantitative proteomic analysis of tumor samples.
  • Demonstrated the capability for integrated proteome and PTM characterization.
  • Validated the approach for comprehensive quantitative proteomic analysis in large clinical cohorts.

Conclusions:

  • The developed quantitative proteomic strategy offers a powerful tool for deep and comprehensive analysis of biological and clinical samples.
  • This approach can yield novel biological insights into disease pathogenesis and therapeutic interventions.
  • The method is adaptable for large-scale studies, including integrated proteome and PTM characterization across diverse patient populations.