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To elucidate the basic structure of biological membranes, experimenltal evidence concerniing the detailed molecular organization of the proteins of membranes is required. This evidence has been almost totally lacking or ambiguous up to the present time. The Cotton. effects due to the peptide bond ultraviolet absorption bands, as studied by ORD and CD, have recently proved extremely valuable in characterizing the molecular conformations of polypeptides and soluble proteins. In this paper, we report the results of ORD and CD studies in the ultraviolet on membrane preparations from human red blood cells and from B. subtilis in several solvent media.

PROTEIN CONFORMATION IN CELL MEMBRANE PREPARATIONS AS STUDIED BY OPTICAL ROTATORY DISPERSION AND CIRCULAR DICHROISM