A probable linking sequence between two transmembrane components of bacteriorhodopsin

Purple membranes from Halobacterium halobium contains predominantly one protein, bacteriorhodopsin, which acts as a light-driven proton pump, and which consists of 7 transmembrane rods of electron scattering density. X-ray diffraction analysis suggests that the rods correspond predominantly to alpha...

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Bibliographic Details
Published in:FEBS letters 1981-12, Vol.136 (1), p.170-174
Main Authors: Katre, Nandini V., Stroud, Robert M.
Format: Article
Language:English
Subjects:
bacteriorhodopsin
chemical modification
Halobacterium halobium
purple membranes
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Summary:Purple membranes from Halobacterium halobium contains predominantly one protein, bacteriorhodopsin, which acts as a light-driven proton pump, and which consists of 7 transmembrane rods of electron scattering density. X-ray diffraction analysis suggests that the rods correspond predominantly to alpha -helical regions, oriented roughly perpendicular to the membrane plane. However, which parts of the sequence are contained in the rods within the bilayer and which correspond to the linking regions between helices is not known. Enzymatic cleavage or chemical modification of the protein, using reagents which preferentially position either into the aqueous, or the lipid phase identify linking or transmembrane regions. The authors describe specific labelling of tyrosines accessible to lactoperoxidase iodination of bacteriorhodopsin from the aqueous phase.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(81)81239-2