The application of surface tension measurements to the study of protein-lipid interactions between a hydrophobic myelin protein (lipophilin) and lipids

Abstract Protein-lipid interactions have been studied using temperature-dependent surface tension experiments. The nature of the lipid and the conformation of the protein were found to be important. Of the lipids studied, sphingomyelin interacted with the β-conformation of a purified, hydrophobic myelin protein (lipophilin) to a greater extent than with the α-helical conformation of the same protein. Cholesterol showed no interaction with protein, and cerebroside only a slight interaction.