Abstract
The myelin sheath derives from the spiral infolding about the axon of a membrane-bound, glial cell process. The major part of the sheath consists of closely packed membrane pairs separated by narrow fluid spaces. The periodic nature of this membrane array makes myelin well suited for examination of its molecular organization by diffraction techniques. Diffraction provides a means of monitoring the separation between membranes and of analyzing the forces and interactions between them. This method, which is nonperturbing, is uniquely suited to analyzing myelin structure and stability in physiologically intact tissue, even in the living animal. X-ray and neutron diffraction results on myelin can be correlated with its chemical composition, its structure as seen by electron microscopy (EM), and its responses to nerve conduction and to physical-chemical treatments. This correlation has led to a description of the average distribution of lipid, protein, and water in the membrane array and to the localization of specific proteins and lipids within the myelin membrane bilayer. It has also led to an understanding of the role of ions in membrane-membrane interactions in myelin and the possible involvement of these ions in nerve conduction.
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Kirschner, D.A., Ganser, A.L., Caspar, D.L.D. (1984). Diffraction Studies of Molecular Organization and Membrane Interactions in Myelin. In: Morell, P. (eds) Myelin. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1830-0_2
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