Electrostatic analysis of charge interactions in proteins

  1. G. P. Tsironis1,2,*,
  2. A. Ciudad1,
  3. J. M. Sancho1

Article first published online: 19 MAY 2009

DOI: 10.1002/qua.22123

Issue

International Journal of Quantum Chemistry

International Journal of Quantum Chemistry

Special Issue: Proceedings of the NATO ARW “Molecular Self-Organization in Micro-, Nano-, and Macro-Dimensions: From Molecules to Water, to Nanoparticles, DNA and Proteins”, Dedicated to Alexander S. Davydov's 95th Birthday

Volume 110, Issue 1, pages 233–241, January 2010

Additional Information

How to Cite

Tsironis, G. P., Ciudad, A. and Sancho, J. M. (2010), Electrostatic analysis of charge interactions in proteins. International Journal of Quantum Chemistry, 110: 233–241. doi: 10.1002/qua.22123

Author Information

  1. 1

    Department d'Estructura i Constituents de la Matéria, Facultat de Física, Universitat de Barcelona, Diagonal 647, E-08028 Barcelona, Spain

  2. 2

    Department of Physics, University of Crete and Institute of Electronic Structure and Laser, FORTH, P. O. Box 2208, Heraklion 71003, Crete, Greece

*Department d'Estructura i Constituents de la Matéria, Facultat de Física, Universitat de Barcelona, Diagonal 647, E-08028 Barcelona, Spain

Publication History

  1. Issue published online: 27 OCT 2009
  2. Article first published online: 19 MAY 2009
  3. Manuscript Accepted: 13 JAN 2009
  4. Manuscript Received: 26 OCT 2008

Funded by

  • Ministerio de Educación y Ciencia (Spain). Grant Numbers: BES-2004-3208, 2006PIV10007

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Keywords:

  • protein electrostatics;
  • charge transfer;
  • kinesin walk;
  • ATP–ADP interaction;
  • Bjerrum length

Abstract

We model proteins as continuous electrostatic media immersed in water to investigate charge mediated processes in their interior. We use a Green's function formalism and find analytical expressions for the electrostatic energy in the vicinity of the protein surfaces. We find that due to image charges generated by the protein dielectric medium embedded in water, the effective electrostatic interaction between the two charges in the interior of the protein has an energy larger than the thermal energy. We focus specifically on kinesin to asses the strength of the electrostatic interaction between ATP and ADP molecules. It is known experimentally that ADP expulsion is correlated to ATP kinesin binding while both processes are essential for the kinesin walk. We estimate that the Bjerrum length in the interior of the kinesin dimer protein is of the order of 4 nm and that the pure electrostatic ATP–ADP interaction is of the order of 3–5 kBT. © 2009 Wiley Periodicals, Inc. Int J Quantum Chem, 2010

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