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Electrostatic complementarity at protein/protein interfaces

A J McCoy1, V Chandana Epa, P M Colman

  • 1Biomolecular Research Institute, Parkville, Victoria, Australia.

Journal of Molecular Biology
|May 2, 1997
PubMed
Summary
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Protein interfaces show significant electrostatic complementarity (EC), not charge complementarity (CC). EC quantifies surface potential correlations, confirming protein association involves complementary electrostatics, unlike CC which measures atomic charge correlations.

Area of Science:

  • Structural Biology
  • Computational Biophysics
  • Protein Interactions

Background:

  • Protein-protein interactions are fundamental to biological processes.
  • Previous studies suggested "charge complementarity" and "electrostatic complementarity" at protein interfaces.
  • Quantitative definitions for these terms were lacking for rigorous investigation.

Purpose of the Study:

  • To develop and apply quantitative measures for charge complementarity (CC) and electrostatic complementarity (EC).
  • To rigorously investigate protein-protein interfaces using these new measures.
  • To reassess the validity of existing assertions regarding charge and electrostatic complementarity in protein association.

Main Methods:

  • Defined charge complementarity (CC) based on correlations of charges on nearest neighbor atoms at the interface.

Related Experiment Videos

  • Defined electrostatic complementarity (EC) based on correlations of surface electrostatic potential at protein interfaces.
  • Applied these measures to 12 protein-protein interfaces and influenza virus neuraminidase epitopes.

    • Main Results:

    • All 12 interfaces showed insignificantly small CC values, suggesting the term is inappropriate in this context.
    • All 12 interfaces exhibited significant EC values, confirming that protein association involves complementary electrostatic potentials.
    • EC did not correlate with interface type or salt bridge number, indicating broader charge contributions.

    Conclusions:

    • The term electrostatic complementarity (EC) is appropriate for describing protein-protein interfaces based on surface potential.
    • Charge complementarity (CC) is not an appropriate descriptor based on nearest-neighbor atomic charge correlations.
    • EC analysis revealed that antibodies can recognize protein surfaces electrostatically in dissimilar ways, even with overlapping epitopes.