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How do two alpha-helices at the constriction point of the Aquaporin 5 transporter protein prevent H3O+ molecules from forming a H+ wire that prevents the transport of H₂O molecules across the membrane? alpha-helices have inverted dipoles that reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds. alpha-helices are amphipathic and can reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds O alpha-helices have inverted dipoles that reorient H3O+ molecules in the channel to form H3O*/ H3O+ H-bonds. alpha-helices have parallel dipoles that align H₂O molecules in the channel to break H₂O/H₂O H-bonds. alpha-helices have Lys residues that reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds.

How do two alpha-helices at the constriction point of the Aquaporin 5 transporter protein prevent H3O+ molecules from forming a H+ wire that prevents the transport of H₂O molecules across the membrane? alpha-helices have inverted dipoles that reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds. alpha-helices are amphipathic and can reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds O alpha-helices have inverted dipoles that reorient H3O+ molecules in the channel to form H3O*/ H3O+ H-bonds. alpha-helices have parallel dipoles that align H₂O molecules in the channel to break H₂O/H₂O H-bonds. alpha-helices have Lys residues that reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds.

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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How do two alpha-helices at the constriction point of the Aquaporin 5 transporter protein prevent H3O+ molecules from forming a H+ wire that prevents the transport of H₂O molecules across the membrane? alpha-helices have inverted dipoles that reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds. alpha-helices are amphipathic and can reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds O alpha-helices have inverted dipoles that reorient H3O+ molecules in the channel to form H3O*/ H3O+ H-bonds. O alpha-helices have parallel dipoles that align H₂O molecules in the channel to break H₂O/H2₂O H-bonds. alpha-helices have Lys residues that reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds.
Transcribed Image Text:How do two alpha-helices at the constriction point of the Aquaporin 5 transporter protein prevent H3O+ molecules from forming a H+ wire that prevents the transport of H₂O molecules across the membrane? alpha-helices have inverted dipoles that reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds. alpha-helices are amphipathic and can reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds O alpha-helices have inverted dipoles that reorient H3O+ molecules in the channel to form H3O*/ H3O+ H-bonds. O alpha-helices have parallel dipoles that align H₂O molecules in the channel to break H₂O/H2₂O H-bonds. alpha-helices have Lys residues that reorient H₂O molecules in the channel to break H₂O/H₂O H-bonds.
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Aquaporin 5

It refers to the water channel protein which is involved in the generation of saliva, tears, and pulmonary secretions. It is involved in the transport of water across the plasma membrane.

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