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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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Deciphering combinatorial post-translational modifications by top-down mass spectrometry.

Jennifer S Brodbelt1

  • 1Department of Chemistry, University of Texas at Austin, Austin, TX 78712, USA.

Current Opinion in Chemical Biology
|July 2, 2022
PubMed
Summary
This summary is machine-generated.

Post-translational modifications (PTMs) diversify proteins, impacting cellular functions. Top-down proteomics using mass spectrometry offers detailed insights into these complex protein modifications and their roles.

Keywords:
Internal ionsIon activationIon-ion reactionsProteoformProteomicsTop-down

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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Post-translational modifications (PTMs) significantly expand protein functional diversity.
  • Combinatorial PTM patterns create protein heterogeneity and mediate interactions.
  • Mass spectrometry has enabled large-scale protein and PTM identification.

Purpose of the Study:

  • To review the benefits of mass spectrometry for analyzing intact proteins.
  • To showcase strategies enhancing top-down proteomics for PTM analysis.
  • To explore the impact of combinatorial PTMs in detail.

Main Methods:

  • Top-down mass spectrometry for intact protein analysis.
  • Characterization of multiple PTMs on individual proteins.
  • Advanced strategies for enhanced proteoform analysis.

Main Results:

  • Top-down proteomics enables comprehensive proteoform cataloging.
  • Detailed mapping of protein sequences and PTM localization is achievable.
  • Insights into the impact of combinatorial PTMs are significantly enhanced.

Conclusions:

  • Top-down proteomics provides unparalleled detail in studying protein modifications.
  • This approach is crucial for understanding protein function, signaling, and regulation.
  • Innovative strategies are advancing the potential of top-down proteomics.