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Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

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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...
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Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

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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...
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Mass Spectrometry of Amines01:15

Mass Spectrometry of Amines

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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...
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Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

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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...
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Chemical Ionization (CI) Mass Spectrometry01:21

Chemical Ionization (CI) Mass Spectrometry

1.5K
The molecular ion peak of a molecule in the mass spectrum provides vital information for molecular identification. However, conventional electron impact ionization can lead to the rapid dissociation of some molecular ions before they reach the detector. A milder ionization method is required to increase the lifetime of such ionized analyte molecules. Chemical ionization (CI) is a gas-phase protonation reaction useful for mass-analyzing analyte molecules that are easily protonated to yield the...
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Mass Spectrometry: Alkene Fragmentation00:59

Mass Spectrometry: Alkene Fragmentation

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Alkenes lose one electron from the unsaturated π bond upon ionization and form stable molecular ions. Further fragmentation of alkenes occurs through three different reaction pathways. The most prominent fragmentation is the cleavage at the allylic position. The resultant allylic carbocation is resonance stabilized. In the mass spectra of terminal alkenes, this fragment appears at a mass-to-charge ratio of 41. In the internal alkenes, where there are two choices of allylic cleavage, the...
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A Guide to Mass Spectrometry-Based Quantitative Proteomics.

Bradley J Smith1, Daniel Martins-de-Souza1,2,3, Mariana Fioramonte4

  • 1Laboratory of Neuroproteomics, Department of Biochemistry and Tissue Biology, Institute of Biology, University of Campinas (UNICAMP), Campinas, Brazil.

Methods in Molecular Biology (Clifton, N.J.)
|December 12, 2018
PubMed
Summary
This summary is machine-generated.

This review compiles quantitative proteomics techniques, including stable isotope labeling and label-free methods, for disease mechanism and biomarker discovery. It offers a practical guide for researchers in quantitative proteomics.

Keywords:
Label-freeMass spectrometryQuantitative proteomicsStable isotope labeling

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Area of Science:

  • Proteomics
  • Biomarker Discovery
  • Post-genomic Era Research

Background:

  • Proteomics enables identification and quantification of thousands of molecules in complex biological samples.
  • Understanding cellular mechanisms of diseases and biological conditions is crucial.
  • Protein biomarkers are essential for disease diagnosis and monitoring.

Purpose of the Study:

  • To provide an up-to-date compilation and comparison of quantitative proteomics techniques.
  • To guide scientists in selecting appropriate methods for their research.
  • To serve as a reference for both novice and experienced researchers in quantitative proteomics.

Main Methods:

  • Comparison of in vitro and in vivo stable isotope labeling techniques.
  • Evaluation of label-free quantitative proteomics methods.
  • Overview of common data acquisition and processing methods in proteomics.

Main Results:

  • Detailed comparison of major quantitative proteomics techniques.
  • Inclusion of essential data acquisition and processing strategies.
  • A comprehensive reference for quantitative proteomics applications.

Conclusions:

  • Quantitative proteomics is a powerful tool in the post-genomic era.
  • The presented compilation aids in understanding and applying various quantification techniques.
  • This resource supports advancements in disease research and biomarker identification.