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Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
11:54

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Tuning probe selectivity for chemical proteomics applications.

Ute Haedke1, Eliane V Küttler, Oliver Vosyka

  • 1Center for Integrated Protein Science Munich, Lehrstuhl für Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, 85354 Freising, Germany.

Current Opinion in Chemical Biology
|January 1, 2013
PubMed
Summary

Covalent chemical probes offer tunable selectivity for investigating proteins. These versatile tools aid in inhibitor discovery and cellular localization studies.

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Area of Science:

  • Chemical biology
  • Proteomics
  • Drug discovery

Background:

  • Covalent chemical probes are essential tools for studying proteins.
  • Their selectivity can be precisely controlled to target specific amino acids, protein classes, or individual proteins.
  • This tunability allows for diverse applications in biological research.

Purpose of the Study:

  • To highlight the capabilities of covalent small molecule probes.
  • To demonstrate how probe selectivity can be modulated for various research needs.
  • To showcase applications in inhibitor screening and imaging.

Main Methods:

  • Designing covalent probes with specific reactive groups.
  • Incorporating recognition elements for enhanced target specificity.

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Last Updated: May 15, 2026

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
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Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
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Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)

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  • Varying probe selectivity for different experimental goals.
  • Main Results:

    • Demonstrated ability to target specific amino acids, protein families, or single protein species.
    • Successfully fine-tuned probes to identify desired proteins among related ones.
    • Showcased applications in inhibitor discovery and protein localization studies.

    Conclusions:

    • Covalent chemical probes are powerful and adaptable tools for proteome investigation.
    • Their tunable selectivity enables precise targeting for diverse biological questions.
    • These probes significantly advance inhibitor discovery and cellular imaging techniques.