A small angle x-ray scattering study of a rhodopsin-lipid complex in hexane.

A small angle x-ray scattering study of a rhodopsin-lipid complex in hexane demonstrates the presence of two distinct particle populations with corresponding radii of gyration of approximately 22 and 160 A. A model based on the existence of inverted lipid micelles surrounding the protein polar moieties while the protein hydrophobic domains act as cross-links between the inverted micelles is presented. It accounts for the results herewith reported and explains most of the properties hitherto characterized for the rhodopsin-lipid complex in hexane.