@article {466,
	title = {The Mechanism of Proton Exclusion in Aquaporin Channels},
	journal = {Proteins},
	volume = {55},
	number = {2},
	year = {2004},
	note = {Ilan, Boaz Tajkhorshid, Emad Schulten, Klaus Voth, Gregory A P41 RR05969/RR/NCRR NIH HHS/United States R01 GM067887/GM/NIGMS NIH HHS/United States R01-GM53148/GM/NIGMS NIH HHS/United States Research Support, U.S. Gov{\textquoteright}t, P.H.S. United States Proteins Proteins. 2004 May 1;55(2):223-8.},
	pages = {223-8},
	abstract = {<p>The mechanism of proton exclusion in aquaporin channels is elucidated through free energy calculations of the pathway of proton transport. The second generation multistate empirical valence bond (MS-EVB2) model was applied to simulate the interaction of an excess proton with the channel environment. Jarzynski{\textquoteright}s equality was employed for rapid convergence of the free energy profile. A barrier sufficiently high to block proton transport is located near the channel center at the NPA motif-a site involved in bi-orientational ordering of the embedded water-wire in absence of the excess proton. A second and lower barrier is observed at the selectivity filter near the periplasmic outlet where the channel is narrowest. This secondary barrier may be essential in filtering other large solutes and cations.</p>},
	keywords = {Aquaporins/*chemistry/*metabolism Biological Transport Cations/metabolism Computer Simulation Escherichia coli Proteins/*chemistry/*metabolism Models, Biological Models, Molecular Protein Conformation *Protons Substrate Specificity Thermodynamics Water/*metabolism},
	doi = {10.1002/prot.20038},
	author = {B. Ilan and E. Tajkhorshid and K. Schulten and G. A. Voth}
}
