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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...

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Related Experiment Video

Updated: May 16, 2026

Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry
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Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry

Published on: April 9, 2021

A nascent proteome study combining click chemistry with 2DE.

Ilya A Osterman1, Alexey V Ustinov, Denis V Evdokimov

  • 1Department of Chemistry, A.N. Belozersky Institute for Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia.

Proteomics
|November 20, 2012
PubMed
Summary

This study introduces a new method for labeling newly synthesized proteins using click chemistry and 2D DIGE. The technique effectively shows how protein synthesis changes in bacterial cells under drug treatment.

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Area of Science:

  • Proteomics
  • Cellular Biology
  • Biochemistry

Background:

  • Investigating dynamic cellular responses requires selective labeling of the nascent proteome.
  • Existing methods may lack the specificity or sensitivity needed for real-time proteome analysis.

Purpose of the Study:

  • To develop and validate a novel method combining click chemistry protein labeling with 2D DIGE (Difference Gel Electrophoresis) for nascent proteome analysis.
  • To assess the impact of protein synthesis inhibition on the bacterial proteome.

Main Methods:

  • Bacterial cells were incubated with a methionine analog (homopropargyl glycine).
  • Nascent proteins were selectively labeled using custom-synthesized Cy3 and Cy5 azides via click chemistry.
  • Labeled proteins were analyzed using 2D DIGE to compare actively growing cells with erythromycin-treated cells.

Main Results:

  • The method revealed a significant reduction in newly synthesized proteins following erythromycin treatment.
  • The total proteome composition remained largely unaffected by the drug.
  • Several proteins exhibiting resistance to erythromycin-induced synthesis inhibition were identified.

Conclusions:

  • The combined click chemistry and 2D DIGE approach is a powerful tool for studying nascent proteome dynamics.
  • This method can effectively identify changes in protein synthesis in response to cellular stress or drug treatment.
  • The findings highlight the specificity of erythromycin and reveal proteins with altered synthesis regulation.