Journal of Computational Electronics

, Volume 7, Issue 1, pp 20–23

Exploration of Na+,K+-ATPase ion permeation pathways via molecular dynamic simulation and electrostatic analysis

  • J. E. Fonseca
  • S. Mishra
  • S. Kaya
  • R. F. Rakowski
Article

Abstract

Biologically-inspired nanodevices can serve as “natural” alternatives to conventional semiconductor devices in many applications from information storage to mechanical rotors. In this work we consider an ATP-powered transmembrane protein, the Na+,K+-ATPase, which has appealing functionality but still lacks an “atomistic” picture capable of elucidating its operation. The vast collection of experimental literature on the Na+,K+-ATPase gives a unique advantage to this protein in developing and validating computational tools. We have performed extensive molecular dynamic simulations of the Na+,K+-ATPase in an accurate biological environment, followed by time-averaged electrostatic analysis, to investigate the ion-binding loci and access/egress pathways that cations may take through the protein as they are transported across the membrane.

Keywords

Na+,K+-ATPase Bionano Homology modeling Electrostatics Molecular dynamics 

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Copyright information

© Springer Science+Business Media LLC 2008

Authors and Affiliations

  • J. E. Fonseca
    • 1
  • S. Mishra
    • 1
  • S. Kaya
    • 1
  • R. F. Rakowski
    • 2
  1. 1.School of EECS, Russ College of Eng. & Tech.Ohio UniversityAthensUSA
  2. 2.Department of Biological SciencesOhio UniversityAthensUSA

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