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Interference is a characteristic phenomenon exhibited by waves. When two electromagnetic waves interact with their peaks and troughs coinciding, a resulting wave with enhanced amplitude is produced. This is known as constructive interference. In this case, the two waves interacting are in phase with each other.
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Related Experiment Video

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Laser Microdissection-Based Protocol for the LC-MS/MS Analysis of the Proteomic Profile of Neuromelanin Granules
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EASI-tag enables accurate multiplexed and interference-free MS2-based proteome quantification.

Sebastian Virreira Winter1,2, Florian Meier1, Christoph Wichmann3

  • 1Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.

Nature Methods
|June 20, 2018
PubMed
Summary
This summary is machine-generated.

We created EASI-tag, a novel labeling reagent for precise quantitative proteomics. This method enables accurate measurement of protein expression differences across six samples using mass spectrometry.

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Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Quantitative proteomics is crucial for understanding biological processes.
  • Existing isobaric labeling methods face challenges with accuracy and interference.
  • Development of novel reagents is needed for improved proteomic analysis.

Purpose of the Study:

  • To introduce EASI-tag, a new class of amine-derivatizing isobaric labeling reagents.
  • To demonstrate the utility of EASI-tag for highly accurate quantitative proteomics.
  • To enable sensitive and reliable quantification of protein expression.

Main Methods:

  • Development of sulfoxide-containing isobaric labeling reagents (EASI-tag).
  • Mass spectrometry-based quantitative proteomics.
  • Low collision energy-induced dissociation of EASI-tag.
  • MS2 level quantification of peptide-coupled reporter ions.

Main Results:

  • EASI-tag reagents enable labeling of amines for quantitative proteomics.
  • EASI-tag labels dissociate at low collision energy, yielding interference-free reporter ions.
  • High yield of reporter ions and efficient isolation of 12C precursors facilitate accurate quantification.
  • Accurate determination of quantitative differences in up to six multiplexed samples.

Conclusions:

  • EASI-tag provides a robust platform for highly accurate quantitative proteomics.
  • The method offers improved sensitivity and accuracy compared to existing techniques.
  • EASI-tag facilitates reliable analysis of complex biological samples.