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

Structural prediction of membrane-bound proteins

P Argos, J K Rao, P A Hargrave
Free article

Structural prediction of membrane-bound proteins

P Argos et al. Eur J Biochem. .
Free article

Abstract

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.

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