Double Helix Formation of Myelin Figures

Abstract

Double helix formation of egg-yolk phosphatidylcholine myelin figures has been studied by use of an optical microscopy. The double helices were looser than a geometrically possible one and the pitchs were related proportionaly to the outer radii of helical myelin figures. The regularity in the winding was explained in terms of the intermembrane binding energy and the bending elastic energy of helical myelin figures.