A study of rhodopsin-detergent micelles by transient electric birefringence.
The hydrodynamic method of transient electric birefringence has been used to study bovine rhodopsin solubilized in two detergents, 0.02% Ammonyx LO and 0.045% digitonin. All measurements are interpreted as the sum of two exponentials by which the relaxation times yield the rotary diffusion coefficients for ellipsoids of revolution. The semi-major and minor axes for prolate ellipsoid models have been calculated and their axial ratio, 6.8, in both detergents, is in line with recent reports on the structure of rhodopsin. Studies on bleached rhodopsin showed a large increase in axial ratio in 0.02% Ammonyx LO.
D001665:Binding Sites; D001718:Birefringence; D003102:Colloids; D003902:Detergents; D004071:Digitalis Glycosides; D004072:Digitonin; D008823:Micelles; D008968:Molecular Conformation; D011485:Protein Binding; D011487:Protein Conformation; D012168:Retinal Pigments; D012243:Rhodopsin
D003102:Colloids; D003902:Detergents; D004071:Digitalis Glycosides; D008823:Micelles; D012168:Retinal Pigments; D012243:Rhodopsin; D004072:Digitonin