(10.5 A)-1 diffraction and transmembrane proteins of erythrocyte ghost membranes.

Four types of erythrocyte ghost membrane (human ghosts, human ghosts stripped of major non-integral membrane proteins, sheep ghosts and agglutinated sheep ghosts) were studied by X-ray diffraction. Specimens of oriented and stacked membranes in an aqueous environment were used for diffraction experiments. Interferences from the membrane profile and from structures within the plane of the membrane were separated in the recorded patterns. Strongly equatorial diffraction bands at (10.5 A)-1 were identified as in-plane diffraction and correlated with probable alpha-helical conformation of the transmembrane polypeptide chains of glycophorin and band III protein.