title: Double helix formation of phosphatidylcholine myelin figures.
abstract: Double helix formation of phosphatidylcholine myelin figures has been studied by use of optical microscopy. The winding of the double helices was looser than a geometrically possible one and the pitch was related proportionally 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.
authors.affiliation: Department of Physics, College of Art & Sciences, Showa University, Yamanashi, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Mishima
authors.forename: K
authors.initials: K
authors.lastname: Fukuda
authors.forename: K
authors.initials: K
authors.lastname: Suzuki
mesh_terms: D008968:Molecular Conformation; D009186:Myelin Sheath / Q000737:chemistry*; D010713:Phosphatidylcholines / Q000737:chemistry*; D013696:Temperature
chemical_list: D010713:Phosphatidylcholines