Electrostatic analysis of charge interactions in proteins

G. P. Tsironis, A. Ciudad, J. M. Sancho

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)233-241
Number of pages9
JournalInternational Journal of Quantum Chemistry
Issue number1
Publication statusPublished - Jan 1 2010


  • ATP-ADP interaction
  • Bjerrum length
  • Charge transfer
  • Kinesin walk
  • Protein electrostatics

ASJC Scopus subject areas

  • Atomic and Molecular Physics, and Optics
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry


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