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Related Concept Videos

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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
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...

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Related Experiment Video

Updated: Jun 1, 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

Deep and highly sensitive proteome coverage by LC-MS/MS without prefractionation.

Suman S Thakur1, Tamar Geiger, Bhaswati Chatterjee

  • 1Department of Proteomics and Signal Transduction, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.

Molecular & Cellular Proteomics : MCP
|May 19, 2011
PubMed
Summary
This summary is machine-generated.

High-resolution liquid chromatography coupled with fast mass spectrometry enables deep proteome characterization without prefractionation. This single-run analysis significantly simplifies proteomic studies while maintaining a systems-wide view.

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Large Scale Non-targeted Metabolomic Profiling of Serum by Ultra Performance Liquid Chromatography-Mass Spectrometry (UPLC-MS)
07:34

Large Scale Non-targeted Metabolomic Profiling of Serum by Ultra Performance Liquid Chromatography-Mass Spectrometry (UPLC-MS)

Published on: March 14, 2013

Related Experiment Videos

Last Updated: Jun 1, 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

Large Scale Non-targeted Metabolomic Profiling of Serum by Ultra Performance Liquid Chromatography-Mass Spectrometry (UPLC-MS)
07:34

Large Scale Non-targeted Metabolomic Profiling of Serum by Ultra Performance Liquid Chromatography-Mass Spectrometry (UPLC-MS)

Published on: March 14, 2013

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • In-depth mass spectrometry (MS)-based proteomics typically requires extensive sample prefractionation, increasing analysis time.
  • Developing faster, more comprehensive proteomic analysis methods is crucial for systems biology.

Purpose of the Study:

  • To evaluate the proteome coverage achievable with single-run liquid chromatography-tandem MS without prefractionation.
  • To assess the sensitivity and dynamic range of this streamlined approach.

Main Methods:

  • Utilized long liquid chromatography runs with high resolution.
  • Employed a mass spectrometer with fast sequencing speed for tandem MS analysis.
  • Performed triplicate single-run analyses on yeast and mammalian cell line samples.

Main Results:

  • Identified 2990 yeast proteins (68% of total) and 5376 proteins in a mammalian cell line per triplicate run.
  • Detected the majority of proteins at sub-femtomole to low attomole levels, indicating high sensitivity.
  • Covered key metabolic pathways, including glycolysis and gluconeogenesis enzymes in yeast.

Conclusions:

  • Single-run liquid chromatography-tandem MS, without prefractionation, provides extensive proteome coverage and high sensitivity.
  • This approach demonstrates a large dynamic range of the MS signal.
  • Further development of single-run analysis can significantly simplify proteomic workflows and maintain a systems-wide perspective.