Structural prediction of membrane-bound proteins

Eur J Biochem. 1982 Nov 15;128(2-3):565-75. doi: 10.1111/j.1432-1033.1982.tb07002.x.


A prediction algorithm based on physical characteristics of the twenty amino acids and refined by comparison to the proposed bacteriorhodopsin structure was devised to delineate likely membrane-buried regions in the primary sequences of proteins known to interact with the lipid bilayer. Application of the method to the sequence of the carboxyl terminal one-third of bovine rhodopsin predicted a membrane-buried helical hairpin structure. With the use of lipid-buried segments in bacteriorhodopsin as well as regions predicted by the algorithm in other membrane-bound proteins, a hierarchical ranking of the twenty amino acids in their preferences to be in lipid contact was calculated. A helical wheel analysis of the predicted regions suggests which helical faces are within the protein interior and which are in contact with the lipid bilayer.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence*
  • Amino Acids
  • Animals
  • Bacteriorhodopsins*
  • Carotenoids*
  • Cattle
  • Lipid Bilayers
  • Membrane Proteins*
  • Protein Conformation*
  • Rhodopsin
  • Structure-Activity Relationship


  • Amino Acids
  • Lipid Bilayers
  • Membrane Proteins
  • Carotenoids
  • Bacteriorhodopsins
  • Rhodopsin