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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...

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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
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Enzyme-cleavable tandem peptides for quantitative studies in MS-based proteomics.

Dominic Winter1, Chien-Wen Hung, Thorsten W Jaskolla

  • 1Molecular Structure Analysis, German Cancer Research Center, Heidelberg, Germany.

Proteomics
|October 24, 2012
PubMed
Summary

A new peptide standard combines two peptides, releasing them in equal amounts after enzymatic digestion. This innovation aids in creating precise peptide mixtures for mass spectrometry (MS) research.

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Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
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Published on: July 31, 2011

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Last Updated: May 17, 2026

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Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
06:09

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

Published on: July 31, 2011

Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Mass Spectrometry

Background:

  • Accurate quantification in mass spectrometry (MS) is crucial for biological and chemical analysis.
  • Generating equimolar peptide mixtures for calibration and validation can be challenging with traditional methods.

Purpose of the Study:

  • To introduce a novel peptide standard for generating exact equimolar peptide mixtures.
  • To demonstrate the utility of this standard in mass spectrometry applications.

Main Methods:

  • A synthetic peptide standard was designed, containing two peptides linked by a proteolytic cleavage site.
  • Enzymatic digestion was employed to release the two peptides.
  • The method was applied to study sequence variation effects on ionization efficiency in electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) MS.

Main Results:

  • The novel standard successfully releases two peptides in a precise one-to-one molar ratio upon enzymatic digestion.
  • This approach allows for the generation of equimolar mixtures of diverse peptides.
  • The method was effectively used to analyze the impact of peptide sequence on ionization efficiency in ESI- and MALDI-MS.

Conclusions:

  • The developed peptide standard offers a reliable method for creating accurate equimolar peptide mixtures.
  • This tool is valuable for fundamental investigations in mass spectrometry, particularly for quantitative analysis.
  • The study highlights the method's applicability in understanding peptide behavior during MS analysis.