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Related Concept Videos

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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MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

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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...
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Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

6.2K
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...
6.2K
Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

2.1K
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...
2.1K
Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

3.0K
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...
3.0K
Inductively Coupled Plasma–Mass Spectrometry (ICP–MS): Overview01:19

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

2.7K
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...
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Related Experiment Video

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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
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FTICR mass spectrometry in proteomics.

Jonas Bergquist1

  • 1Institute of Chemistry, Department of Analytical Chemistry, Biomedical Center, Uppsala University, PO Box 599, SE-751 24 Uppsala, Sweden. jonas.bergquist@kemi.uu.se

Current Opinion in Molecular Therapeutics
|July 23, 2003
PubMed
Summary

High-resolution mass spectrometry (MS) offers rapid, accurate protein identification for complex biological samples. This review highlights advanced MS techniques, including Fourier transform ion cyclotron resonance MS, for modern proteomics.

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Mass spectrometry (MS) is crucial for analyzing complex biological samples.
  • Proteomics, the study of protein expression, is a rapidly expanding field within MS applications.
  • Traditional methods like 2D-SDS-PAGE have limitations in speed and scope.

Purpose of the Study:

  • To review the application of high-resolution mass spectrometry in proteomics.
  • To present advanced analytical tools for protein identification.
  • To discuss 'top down' and 'bottom up' proteomic strategies using advanced MS.

Main Methods:

  • High-resolution Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS).
  • Multidimensional liquid separations coupled with MS.

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Large-scale Top-down Proteomics Using Capillary Zone Electrophoresis Tandem Mass Spectrometry
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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
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  • 'Top down' and 'bottom up' proteomic analysis strategies.

    • Main Results:

    • FT-ICR MS enables accurate and sensitive protein identification.
    • Coupled separation techniques enhance proteomic coverage.
    • Advanced MS approaches overcome limitations of traditional methods.

    Conclusions:

    • High-resolution MS, particularly FT-ICR MS, is a powerful tool for modern proteomics.
    • These techniques facilitate rapid screening and low sample consumption.
    • The presented methods advance the study of complex biological systems.