Nuclear Magnetic Resonance Spectroscopic Studies of Erythrocyte Membranes

Abstract

THE nature of molecular interactions in the lipoprotein complexes of biological membranes has been a subject under active enquiry for many years. The classical Davson-Danielli paucimolecular model¹ postulates apolar mutual interaction between the lipid molecules and electrostatic binding of the lipid with the structural protein. Although this model has received support from biophysical studies, especially on myelin^2,3, there is other experimental evidence which suggests that extensive hydrophobic binding may occur between lipids and proteins, for example, from studies on mitochondria^4,5, halobacterium halobium⁶, erythrocyte ghosts⁷, plasma membrane fragments of Ehrlich ascites cells (D. F. H. Wallach and P. H. Zahler, personal communication) and chloroplast lamellae⁸.