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Originally published as Biophys J. BioFAST on March 31, 2006.
doi:10.1529/biophysj.106.084061
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Biophysical Journal 90:L73-L75 (2006)
© 2006 The Biophysical Society

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

Hanning Chen, Yujie Wu and Gregory A. Voth

Center for Biophysical Modeling and Simulation, Department of Chemistry, University of Utah, Salt Lake City, Utah, 84112-0850

Correspondence: Address reprint requests and inquiries to Gregory A. Voth, Tel.: 801-581-7272; Fax: 801-581-4353; E-mail: voth{at}chem.utah.edu.

The permeation free-energy profile and maximum ion conductance of proton transport 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 proton transport 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).




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