Biophysics of structure and mechanism

, Volume 9, Issue 4, pp 235–244

The structure of bovine rhodopsin

Authors

  • P. A. Hargrave
    • Department of Medical Biochemistry, School of MedicineSouthern Illinois University
    • Department of Chemistry and Biochemistry, College of ScienceSouthern Illinois University
  • J. H. McDowell
    • Department of Medical Biochemistry, School of MedicineSouthern Illinois University
  • Donna R. Curtis
    • Department of Medical Biochemistry, School of MedicineSouthern Illinois University
  • Janet K. Wang
    • Department of Medical Biochemistry, School of MedicineSouthern Illinois University
  • Elizabeth Juszczak
    • Department of Medical Biochemistry, School of MedicineSouthern Illinois University
  • Shao-Ling Fong
    • Department of Medical Biochemistry, School of MedicineSouthern Illinois University
  • J. K. Mohana Rao
    • Department of Biological SciencesPurdue University
  • P. Argos
    • Department of Biological SciencesPurdue University
Article

DOI: 10.1007/BF00535659

Cite this article as:
Hargrave, P.A., McDowell, J.H., Curtis, D.R. et al. Biophys. Struct. Mechanism (1983) 9: 235. doi:10.1007/BF00535659

Abstract

We have isolated 16 peptides from a cyanogen bromide digest of rhodopsin. These cyanogen bromide peptides account for the complete composition of the protein. Methionine-containing peptides from other chemical and enzymatic digests of rhodopsin have allowed us to place the cyanogen bromide peptides in order, yielding the sequence of the protein. We have completed the sequence of most of the cyanogen bromide peptides. This information, in conjunction with that from other laboratories, forms the basis for our prediction of the secondary structure of the protein and how it may be arranged in the disk membrane.

Key words

Rhodopsin Amino acid sequence Secondary structure Topography Disk membrane

Copyright information

© Springer-Verlag 1983