@article {627,
	title = {Structure and Dynamics of Hydronium in the Ion Channel Gramicidin A},
	journal = {Biophys J},
	volume = {70},
	number = {5},
	year = {1996},
	note = {Sagnella, D E Voth, G A Research Support, Non-U.S. Gov{\textquoteright}t United states Biophysical journal Biophys J. 1996 May;70(5):2043-51.},
	pages = {2043-51},
	abstract = {<p>The effects of the hydronium ion, H(3)0+, on the structure of the ion channel gramicidin A and the hydrogen-bonded network of waters within the channel were studied to help elucidate a possible mechanism for proton transport through the channel. Several classical molecular dynamics studies were carried out with the hydronium in either the center of a gramicidin monomer or in the dimer junction. Structural reorganization of the channel backbone was observed for different hydronium positions, which were most apparent when the hydronium was within the monomer. In both cases the average O-O distance between the hydronium ion and its nearest neighbor water molecule was found to be approximately 2.55 A, indicating a rather strong hydrogen bond. Importantly, a subsequent break in the hydrogen-bonded network between the nearest neighbor and the next-nearest neighbor(approximately 2.7 -3.0 A) was repeatedly observed. Moreover, the carbonyl groups of gramicidin A were found to interact with the charge on the hydronium ion, helping in its stabilization. These facts may have significant implications for the proton hopping mechanism. The presence of the hydronium ion in the channel also inhibits to some degree the reorientational motions of the channel water molecules.</p>},
	keywords = {Alanine Dimerization Gramicidin/*chemistry Hydrogen Bonding *Ion Channels Kinetics Models, Molecular Onium Compounds/*chemistry *Protein Conformation Tryptophan Valine},
	doi = {10.1016/S0006-3495(96)79773-4},
	author = {Sagnella, D. E. and G. A. Voth}
}
