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Ion-dipole interactions and their functions in proteins.

Katherine H Sippel1, Florante A Quiocho1

  • 1Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, 77030.

Protein Science : a Publication of the Protein Society
|April 14, 2015
PubMed
Summary

Ion-dipole interactions, crucial for protein function, involve ions and protein dipoles. This review highlights their underappreciated roles in biological systems.

Keywords:
ABC transport receptorsAP180IMP dehydrogenaseIon-dipole interactionSNAREion channelphage tail proteinsserine protease

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Ion-dipole interactions are electrostatic attractions between ions and dipolar groups in proteins.
  • These interactions occur via hydrogen bonds or coordination bonds.
  • They are prevalent in various protein structures, including transporters, ion channels, enzyme active sites, and protein-protein interfaces.

Purpose of the Study:

  • To define ion-dipole interactions in biological macromolecules.
  • To review the functional significance of these interactions in proteins.
  • To provide examples of their roles in biological processes.

Main Methods:

  • Data mining of the Protein Data Bank (PDB) to identify proteins with ion-dipole interactions.
  • Literature review to synthesize current understanding of these interactions.

Main Results:

  • Ion-dipole interactions are frequently observed in diverse protein structures.
  • Their functional importance in protein mechanisms is often underestimated.
  • Specific examples illustrating their roles are presented.

Conclusions:

  • Ion-dipole interactions are fundamental to protein structure and function.
  • Further research is needed to fully appreciate their significance.
  • Understanding these interactions can advance fields like drug design and protein engineering.