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Related Concept Videos

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...
SDS-PAGE01:27

SDS-PAGE

Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed  polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...

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Related Experiment Video

Updated: Jul 4, 2026

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Protein processing characterized by a gel-free proteomics approach.

Petra Van Damme1, Francis Impens, Joël Vandekerckhove

  • 1Ghent University, Ghent, Belgium.

Methods in Molecular Biology (Clifton, N.J.)
|July 2, 2008
PubMed
Summary

This study introduces a novel gel-free proteomics method for isolating N-terminal peptides. This technique aids in analyzing protein expression and protease activity in degradomics research.

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Area of Science:

  • Proteomics
  • Biochemistry
  • Analytical Chemistry

Background:

  • Proteomics research often requires specific isolation of protein fragments.
  • Existing methods may lack efficiency or specificity for N-terminal peptide analysis.

Purpose of the Study:

  • To develop a gel-free, peptide-centric method for isolating N-terminal peptides.
  • To enable characterization of protein expression and protease activity.

Main Methods:

  • Utilized diagonal chromatography for peptide separation.
  • Introduced altered chemical properties to N-terminal peptides for differential retention.
  • Employed mass spectrometry for peptide characterization.

Main Results:

  • Successfully isolated representative N-terminal peptides and their fragments.
  • Demonstrated altered column retention for modified internal peptides.
  • Enabled identification of neo-N-termini generated by protease cleavage.

Conclusions:

  • The developed gel-free proteomics approach is effective for N-terminal peptide isolation.
  • This technology is applicable to differential proteome surveys and protease degradomics.
  • Facilitates the study of protease specificity and substrate repertoires.