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| | Structure, Dynamics, and Function of Aquaporins |
 | | Water molecules passing the channel are forced, by the protein's electrostatic forces, to flip at the center of the channel (see the animation), thereby breaking the alternative donor-acceptor arrangement that is necessary for proton translocation (read the complete story in our Science paper). |
 | | Analysis of hydrogen bond interactions of the substrate with the interior of the channel also explained for the first time why these channels incorporate in their architecture two characteristic loops, including energetically unfavorable secondary structure elements, which are conserved in the whole aquaporin family (Jensen et al., Structure, 2001). |
 | | In order to directly compare the results of MD simulations with biochemical measurements of the conductivity of membrane water channels, in which osmotic pressure gradients are used to induce the flow of water across the membrane, we developed a new methodology for MD simulations. |
| www.ks.uiuc.edu /Research/aquaporins (1783 words) |
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