Abstract
Aquaporins are membrane proteins responsible for the permeation of water and other solutes through the cell membrane. They arrange in a tetrameric conformation, where each monomer acts as a highly efficient single-file water channel. The x-ray structure of the yeast aquaporin (Aqy1), recently found at a very high resolution (1.15 Angstrom), revealed the conformation of the extended N-terminus - an unusual feature within the family of aquaporins - occluding the water pore. In contrast, functional assays with spheroplast of P.
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