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Related Concept Videos

Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
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...
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...
MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
Mass Spectrometers01:16

Mass Spectrometers

This lesson details the instrumentation of a mass spectrometer—a physical instrument to perform mass spectrometry on analyte molecules and record the characteristic mass spectra. This is achieved via three chief functions:

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A Strategy for Sensitive, Large Scale Quantitative Metabolomics
14:18

A Strategy for Sensitive, Large Scale Quantitative Metabolomics

Published on: May 27, 2014

Mass spectrometry-based quantification.

Leroi V DeSouza1, K W Michael Siu

  • 1Department of Chemistry and Centre for Research in Mass Spectrometry, York University, 4700 Keele Street, Toronto, Ontario, Canada M3J 1P3.

Clinical Biochemistry
|October 30, 2012
PubMed
Summary
This summary is machine-generated.

This review covers mass spectrometry quantification methods in proteomics, detailing labeled and unlabeled approaches. The best method depends on experimental context and cost.

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Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Mass spectrometry is a key technology for protein quantification.
  • Accurate quantification is crucial for understanding biological processes.

Purpose of the Study:

  • To review common mass spectrometry-based quantification methods in proteomics.
  • To compare labeled and unlabeled quantification strategies.

Main Methods:

  • Discusses labeled approaches using mass-tagging (chemical or metabolic).
  • Explains unlabeled approaches relying on run-to-run comparisons.
  • Highlights commercial labeling reagents and their characteristics.

Main Results:

  • Labeled methods pool samples, reducing run-to-run variability.
  • Unlabeled methods assume reproducible separation and similar sample composition.
  • Various commercial labeling reagents are available with distinct pros and cons.

Conclusions:

  • Method selection balances financial factors with experimental needs.
  • Both labeled and unlabeled techniques offer valuable proteomic quantification strategies.