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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...
Rapid Identification of Pathogens01:25

Rapid Identification of Pathogens

MALDI-TOF MS has transformed clinical microbiology by offering a rapid and reliable method for pathogen identification. The traditional approach to microbial identification typically involves time-consuming culture techniques and biochemical tests, which can delay the initiation of appropriate antimicrobial therapy. MALDI-TOF MS avoids these delays by using characteristic ribosomal protein mass patterns of microbial cells, enabling accurate species-level identification within minutes.Principle...
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...

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Related Experiment Video

Updated: Jun 22, 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

Multidimensional protein identification technology for clinical proteomic analysis.

Pierluigi Mauri1, Michaela Scigelova

  • 1Institute for Biomedical Technologies, Segrate (Milan), Italy. pierluigi.mauri@itb.cnr.it

Clinical Chemistry and Laboratory Medicine
|June 17, 2009
PubMed
Summary
This summary is machine-generated.

Proteomics research uses advanced separation techniques to find disease biomarkers. This review highlights multidimensional protein identification technology (Mupid) as a promising non-gel-based approach for mass spectrometry analysis.

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TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis
07:44

TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis

Published on: June 8, 2020

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Last Updated: Jun 22, 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

TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis
07:44

TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis

Published on: June 8, 2020

Area of Science:

  • Proteomics
  • Biomarker Discovery
  • Analytical Chemistry

Background:

  • Proteomics technologies offer vast data for identifying disease-specific biomarkers in biological samples.
  • Traditional two-dimensional polyacrylamide gel electrophoresis (2DE) has limitations in automation, sensitivity, and throughput for complex proteome analysis.

Purpose of the Study:

  • To review recent advances in multidimensional peptide separation techniques compatible with mass spectrometry (MS).
  • To highlight the potential of non-gel-based separation methods for improved proteome analysis.
  • To focus on two-dimensional liquid chromatography coupled with MS (multidimensional protein identification technology) as a key approach.

Main Methods:

  • Review of recent literature on multidimensional peptide separation techniques.
  • Discussion of gel electrophoresis, isoelectric focusing, capillary electrophoresis, and liquid chromatography.
  • Emphasis on two-dimensional liquid chromatography coupled with MS.

Main Results:

  • Non-gel-based separation technologies are advancing for resolving complex protein and peptide mixtures.
  • Multidimensional protein identification technology (Mupid) shows significant promise for MS-based proteomic studies.
  • These advanced techniques aim to overcome the limitations of traditional 2DE methods.

Conclusions:

  • Multidimensional separation techniques, particularly Mupid, are crucial for enhancing biomarker discovery in proteomics.
  • Continued development of non-gel-based methods is essential for improving automation, sensitivity, and throughput in proteomic analyses.
  • The integration of advanced separation with MS represents the future of comprehensive proteome analysis.