Membrane proteins as light-energy transducers

✍ Scribed by Yu. A. Ovchinnikov

• Book ID: 102764846
• Publisher: Wiley (John Wiley & Sons)
• Year: 1985
• Tongue: English
• Weight: 641 KB
• Volume: 24
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360240113

✦ Synopsis

Monoclonal antibodies to different parts of bacteriorhodopsin were raised to define its topography in the membrane. It is shown that the amino acid residue Glu 194 is a part of an antigenic determinant and should be located on the membrane surface. We found that the removal of the C-terminal 17 amino acid sequence does not affect the efficiency of the proton transport in bacteriorhodopsin. From a combination of proteolysis and secondary structure prediction methods an experimentally testable structural model for bovine rhodopsin is presented. The complete amino acid sequence of the transducin y-subunit consisting of 69 residues was determined.