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Related Experiment Video

Updated: Oct 12, 2025

Capillary Electrophoresis-based Hydrogen/Deuterium Exchange for Conformational Characterization of Proteins with Top-down Mass Spectrometry
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Quantifying charge state heterogeneity for proteins with multiple ionizable residues.

Martin J Fossat1, Ammon E Posey1, Rohit V Pappu1

  • 1Department of Biomedical Engineering and Center for Science & Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, Missouri.

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|November 26, 2021
PubMed
Summary

The q-canonical ensemble method analyzes protein charge states by separating proton binding from conformational changes. This approach quanties pH-dependent mesostate populations, aiding in understanding protein behavior.

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Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Chemistry

Background:

  • Ionizable residues influence protein structure and function through proton exchange.
  • Protonation extent depends on solution pH and local residue environments.
  • Charge microstates represent distinct protonation patterns.

Purpose of the Study:

  • To introduce and apply the q-canonical ensemble for analyzing potentiometric titrations.
  • To decouple net proton binding from conformational and proton arrangement effects.
  • To determine mesostate pKa values and pH-dependent mesostate populations in proteins.

Main Methods:

  • Utilizing the q-canonical ensemble framework to analyze potentiometric titration data.
  • Grouping charge microstates into mesostates based on net charge.
  • Applying the formalism to proteins with repetitive Lys and Glu residues.

Main Results:

  • Successfully decoupled net proton binding/release from conformational considerations.
  • Determined underlying mesostate pKa values for repetitive residue patterns.
  • Estimated relative mesostate populations as a function of pH.

Conclusions:

  • The q-canonical ensemble provides a powerful method for analyzing protein charge equilibria.
  • This approach offers quantitative, protein-specific descriptions of pH-dependent mesostate populations.
  • The method is crucial for understanding how charge states impact protein conformational, binding, and phase equilibria.