17.9 How were cubic lipid phases important for the determination of the structure of
bacteriorhodopsin?
17.10 What questions remained after the determination of the structure of bacteriorhodopsin
by electron microscopy?
17.11 Why is the presence of water molecules important in bacteriorhodopsin?
17.12 Why does bacteriorhodopsin function as a light-activated proton switch?
17.13 What similarities are found for rhodopsin, bacteriorhodopsin, halorhodopsin, and sensory
rhodopsin?
17.14 Describe the functional differences between bacteriorhodopsin and sensory rhodopsin.
17.15 What is the role of the transducer proteins in sensory rhodopsin?
17.16 How can halorhodopsin transfer a chloride ion without the presence of a channel?
17.17 Explain the role of dipole interactions in triggering proton transfer in bacteriorhodopsin.
17.18 Contrast the role of dipole interactions in triggering proton transfer in bacteriorhodopsin
compared to chloride transfer in halorhodopsin.
17.19 How is the cellular location of malanopsin different from that of the other photoreceptors
of the eye?
17.20 Why does the mutation of certain amino acid residues, such as Asp-85, result in a struc-
turally intact but nonfunctional bacteriorhodopsin?
17.21 Compare and contrast the proton-switch model of bacteriorhodopsin and halorhodopsin.
singke
(singke)
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