Infrared Spectra and the Chain Organization of Erythrocyte Membranes

Abstract

Changes in the intensity of the 720 cm(-1) band were followed in the infrared spectra of the human erythrocyte membrane and its total lipid extract, recorded at various temperatures. These changes are interpreted in terms of the configuration of the lipid hydrocarbon chains within the membrane. Effects of temperature, sonication, removal of lipids, and organic solvents on the amide I and II bands, associated with protein conformations, were also studied.