Abstract
The effect of single amino acid substitution and membrane bound cations on the orientational behavior of purple membrane fragments was studied by electric light scattering. A direct experimental evidence for the contribution of the surface-exposed Asp38 amino acid residue of bacteriorhodopsin to the membrane electric dipole moments is presented. The strong drop of the permanent electric dipole moment upon deionization of wild type bR and D38R mutant indicates the cation binding sites location on the extracelluar membrane surface.
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