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pH dependence of antibody/lysozyme complexation

C J Gibas1, S Subramaniam, J A McCammon

  • 1Department of Molecular and Integrative Physiology, Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

Biochemistry
|January 31, 1998
PubMed
Summary

Protein complex formation is sensitive to pH and ionic strength. This study reveals how environmental factors like structural changes and residue positioning influence the energetics of hen egg lysozyme-antibody interactions.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biophysics

Background:

  • Protein-protein interactions are crucial in biological systems.
  • The association of proteins is often modulated by solution conditions such as pH and ionic strength.
  • Titratable residues at the interface significantly impact complex stability under varying conditions.

Purpose of the Study:

  • To investigate the pH-dependent energetics of association between hen egg lysozyme and monoclonal antibodies.
  • To analyze the influence of environmental factors on the titration behavior and energetics of protein-antibody complexes.
  • To elucidate the role of specific factors like structural rearrangements and residue geometry in modulating complex formation.

Main Methods:

  • Continuum electrostatics methods were employed to calculate pH-dependent association energetics.

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  • Detailed analysis of energetic contributions was performed.
  • Modeled structures of mutant complexes were studied to dissect individual factor contributions.

    • Main Results:

    • Conserved charged-residue interactions are key to association, but their energetics are significantly influenced by the local environment.
    • Factors such as minor structural rearrangements, buried interfacial area, dielectric environment, and residue geometry affect titration behavior.
    • Mutant complex modeling provided insights into the contribution of individual factors.

    Conclusions:

    • The energetics of protein-antibody association are highly sensitive to the microenvironment of titratable residues.
    • Understanding these environmental influences is critical for predicting and engineering protein complex stability.
    • This work highlights the interplay between intrinsic residue properties and extrinsic factors in governing protein interactions.