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• W2025459574 abstract "The atomic structures of a transmembrane water plus glycerol conducting channel (GlpF), and now of aquaporin Z (AqpZ) from the same species, Escherichia coli, bring the total to three atomic resolution structures in the aquaporin (AQP) family. Members of the AQP family each assemble as tetramers of four channels. Common helical axes support a wider channel in the glycerol plus water channel paradigm, GlpF. Water molecules form a single hydrogen bonded file throughout the 28 A long channel in AqpZ. The basis for absolute exclusion of proton or hydronium ion conductance through the line of water is explored using simulations." @default.
• W2025459574 created "2016-06-24" @default.
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• W2025459574 date "2003-10-23" @default.
• W2025459574 modified "2023-10-13" @default.
• W2025459574 title "Selectivity and conductance among the glycerol and water conducting aquaporin family of channels" @default.
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• W2025459574 doi "https://doi.org/10.1016/s0014-5793(03)01195-5" @default.
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