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Related Concept Videos

Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...
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...
Inductively Coupled Plasma–Mass Spectrometry (ICP–MS): Overview01:19

Inductively Coupled Plasma–Mass Spectrometry (ICP–MS): Overview

In inductively coupled plasma–mass spectrometry (ICP–MS), an inductively coupled plasma (ICP) torch is used as an atomizer and ionizer. Solid samples are dissolved and volatilized before being introduced into the high-temperature argon plasma, while solution samples are nebulized and passed through the high-temperature argon plasma. Plasma dissociates the analytes and ionizes their component atoms to form a mixture of positive ions and molecular species. The positive ions are then passed on to...
Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
High-Resolution Mass Spectrometry (HRMS)01:15

High-Resolution Mass Spectrometry (HRMS)

The resolution of a mass spectrometer depends on the efficiency of separating ions with different ion masses. The mass of an atom is approximated to the sum of the masses of protons and neutrons inside, considering the masses of protons and neutrons as equal. However, the masses of the proton (1.6726 × 10−24 g) and neutron (1.6749 × 10−24 g) are not truly equal. There is a minor error in the expression of atomic masses relative to the simplest atom of hydrogen. For example, the mass of helium...

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Related Experiment Video

Updated: Jun 13, 2026

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

Protein quantitation using isotope-assisted mass spectrometry.

Kelli G Kline1, Michael R Sussman

  • 1Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.

Annual Review of Biophysics
|May 14, 2010
PubMed
Summary

Heavy isotope labeling in organisms, like nitrogen-15 (15N), offers superior controls for mass spectrometry. This technique enhances the accuracy of quantifying proteome changes in biological research.

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Last Updated: Jun 13, 2026

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

  • Proteomics
  • Biotechnology
  • Analytical Chemistry

Background:

  • Cellular proteomes change due to genetic, chemical, and environmental factors.
  • Mass spectrometry advancements improve measurement accuracy and throughput.
  • Heavy isotope internal standards are emerging as crucial tools.

Purpose of the Study:

  • To discuss the theory and practice of using heavy isotope-labeled organisms.
  • To review recent biological applications of this technology.

Main Methods:

  • Utilizing mammals grown with near-complete replacement of common elements (e.g., 15N) with heavy isotopes.
  • Employing isotopically labeled organisms as internal standards.
  • Applying mass spectrometry for proteome quantification.

Main Results:

  • Heavy isotope-labeled organisms serve as effective controls.
  • These controls help isolate and identify experimental variables like extraction efficiencies.
  • The technology enables more accurate proteome change quantification.

Conclusions:

  • Heavy isotope labeling is a powerful technique in modern biological research.
  • It significantly improves the reliability of proteomic studies.
  • This method has broad applications in understanding cellular responses.