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dc.contributor.authorFujiyoshi, Yoshinori
dc.contributor.authorEngel, Andreas
dc.contributor.authorHeymann, J. Bernard
dc.contributor.authorAgre, Peter
dc.contributor.authorWalz, Thomas
dc.contributor.authorHirai, Teruhisa
dc.contributor.authorMitsuoka, Kaoru
dc.contributor.authorMurata, Kazuyoshi
dc.date.accessioned2010-05-13T14:44:32Z
dc.date.available2010-05-13T14:44:32Z
dc.date.issued2000-10-05
dc.identifier.citationNature 407, 599-605 (5 October 2000) | doi:10.1038/35036519en_US
dc.identifier.urihttp://jhir.library.jhu.edu/handle/1774.2/34112
dc.description.abstractHuman red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple highly conserved amino-acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues that permit rapid water transport, whereas the water selectivity is due to a constriction of the pore diameter to about 3 A over a span of one residue. The atomic model provides a possible molecular explanation to a longstanding puzzle in physiology-how membranes can be freely permeable to water but impermeable to protons.en_US
dc.language.isoen_USen_US
dc.publisherNature Publishing Groupen_US
dc.subjectWater/chemistryen_US
dc.subjectAquaporins/chemistryen_US
dc.titleStructural determinants of water permeation through aquaporin-1en_US
dc.typeArticleen_US


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