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Related Concept Videos

¹H NMR of Labile Protons: Deuterium (²H) Substitution00:48

¹H NMR of Labile Protons: Deuterium (²H) Substitution

This lesson illustrates the role of deuterium substitution in simplifying the NMR spectrum of compounds comprising labile protons. One method employed is the use of deuterium. Amongst the three isotopes of hydrogen, deuterium (2H) has a nucleus composed of one proton and one neutron. When the D2O solvent is added to a pure dry ethanol solution, its labile proton is substituted with deuterium.
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
Mass Spectrometry of Amines01:15

Mass Spectrometry of Amines

In mass spectroscopy, amines undergo fragmentation to give parent ions with odd molecule weights. This observed mass spectrum follows the nitrogen rule; a molecule with an odd number of nitrogen atoms produces a molecular ion with an odd molecular weight. Amines undergo fragmentation through α cleavage, producing nitrogen-containing cations—iminium ions—and alkyl radicals. Mass spectra of aromatic and cyclic aliphatic amines exhibit strong molecular ion peaks, but acyclic aliphatic amines show...

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Related Experiment Video

Updated: Jun 10, 2026

Enhanced Sample Multiplexing of Tissues Using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)
09:06

Enhanced Sample Multiplexing of Tissues Using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)

Published on: May 1, 2017

Deuterium isobaric amine-reactive tags for quantitative proteomics.

Junxiang Zhang1, Yan Wang, Shuwei Li

  • 1Institute of Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Drive, Rockville, Maryland 20850, USA.

Analytical Chemistry
|August 19, 2010
PubMed
Summary

A new deuterium ((2)H) isobaric amine-reactive tag (DiART) enables accurate quantitative proteomics. This cost-effective method shows negligible isotope effects and high performance for large-scale studies.

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Amide Hydrogen/Deuterium Exchange & MALDI-TOF Mass Spectrometry Analysis of Pak2 Activation
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Amide Hydrogen/Deuterium Exchange & MALDI-TOF Mass Spectrometry Analysis of Pak2 Activation

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Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
11:53

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling

Published on: July 1, 2014

Related Experiment Videos

Last Updated: Jun 10, 2026

Enhanced Sample Multiplexing of Tissues Using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)
09:06

Enhanced Sample Multiplexing of Tissues Using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)

Published on: May 1, 2017

Amide Hydrogen/Deuterium Exchange & MALDI-TOF Mass Spectrometry Analysis of Pak2 Activation
07:15

Amide Hydrogen/Deuterium Exchange & MALDI-TOF Mass Spectrometry Analysis of Pak2 Activation

Published on: November 26, 2011

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
11:53

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling

Published on: July 1, 2014

Area of Science:

  • Proteomics
  • Mass Spectrometry
  • Biochemistry

Background:

  • Quantitative proteomics is crucial for understanding biological systems.
  • Accurate and cost-effective labeling techniques are needed for large-scale proteomic analyses.

Purpose of the Study:

  • To introduce and evaluate a novel deuterium ((2)H) isobaric amine-reactive tag (DiART) for quantitative proteomics.
  • To assess the performance of DiART on LTQ-Orbitrap mass spectrometers.

Main Methods:

  • Peptide labeling with DiART.
  • Analysis using electrospray ionization (ESI)-based LTQ-Orbitrap mass spectrometry.
  • Hybrid collision-induced dissociation (CID)-higher energy C-trap dissociation (HCD) and electron-transfer dissociation (ETD)-HCD acquisition methods.

Main Results:

  • DiART labeling demonstrated negligible (2)H isotope effects during tandem mass spectrometry (MS/MS) and chromatography.
  • High confidence identification and accurate quantification of DiART-labeled peptides were achieved.
  • A novel data analysis approach enabled reliable measurement of peptide phosphorylation.

Conclusions:

  • DiART is a robust and cost-effective reagent for quantitative proteomics.
  • The DiART method exhibits excellent performance on LTQ-Orbitrap instruments.
  • This technique facilitates large-scale quantitative proteomic measurements and phosphoproteomics.