Correspondence of phases of electrogenesis, photocycle transitions, and proton transfer with the proton transporting groups of bacteriorhodopsin was studied. The structure of bacteriorhodopsin was considered by the file 1c3w and projections of sites of the proton movement pathway onto the normal to the purple membrane were measured. The dielectric permeability of the terminal site of the semichannel Schiff base --> external surface of the purple membrane was noticeably higher than in the center of the membrane.
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- The bacteriorhodopsin from purple membranes is a light-sensing protein crucial for ion transport and has potential applications in optogenetics and bioelectronics due to its unique properties.
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