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Biophys. J. BioFAST: First Published March 31, 2006. doi:10.1529/biophysj.106.084061
© 2006 by the Biophysical Society.

A more recent version of this article appeared on May 15, 2006.
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BIOPHYSICAL LETTERS

Origins of Proton Transport Behavior from Selectivity Domain Mutations of the Aquaporin-1 Channel

Hanning Chen 1, Yujie Wu 1 and Gregory A. Voth 1*

1 University of Utah

* To whom correspondence should be addressed. E-mail: voth{at}chem.utah.edu.

Submitted on February 25, 2006
Revised on March 6, 2006
Accepted on 13 March 2006


  Abstract
The permeation free energy profile, and maximum ion conductance of proton transport (PT) along the channel of three aquaporin-1 (AQP1) mutants (H180A/R195V, H180A, and R195V) are calculated via molecular dynamics simulations and Poisson-Nernst-Planck theory. The proton dynamics was described by the multistate empirical valence bond (MS-EVB) model. The results reveal three major contributions to the overall free energy barrier for PT in AQP1: (1) the bipolar field, (2) the electrostatic repulsion due to the Arg-195 residue, and (3) the dehydration penalty due to the narrow channel pore. The double mutation (H180A/R195V) drastically drops the overall free-energy barrier by roughly 20 kcal/mol via simultaneously relaxing the direct electrostatic interaction (by R195V) and dehydration effect (by H180A).

Key Words: aquaporin channel, molecular dynamics, mutations, proton conductance, proton transport




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Copyright © 2006 by the Biophysical Society.