A laser Raman spectroscopic investigation of phospholipid and protein configurations in hemoglobin-free erythrocyte ghosts.

Configurations of both the protein and lipid components of human red blood cell ghosts are examined by laser Raman spectroscopy. Protein configuration is estimated from bands observed in the Amide III region at 1240-1267 cm-1 in water and the Amide I' region at 1630-1670 cm-1 observed in 2H2O. The protein fraction appears to contain 40-55 percent alpha-helix with little beta-configuration. The hydrophobic side chains of the phospholipid component, as interpreted from the 1060-1130 cm-1 C-C stretching region, are estimated to contain 55-65 percent all-trans rigid configuration. These estimated are within the limits set by other physical techniques.