Membrane-stacking Properties of Myelin Proteins
Myelin is the lipid-rich insulative structure responsible for nerve impulse acceleration. It's a biologically novel environment composed of stacked lipid bilayers held together by specific adhesion proteins in very low aqueous content. The very detailed mechanisms of myelin formation and stability are unknown and of medical relevance, as several compact myelin proteins are involved in changes in myelin morphology and disease. We propose a 6-day experiment at the ILL D17 reflectometer, which is an excellent instrument for the plans at hand: we want to measure three different recombinantly produced myelin proteins in artificially stacked lipid bilayers on a solid-liquid interface, which mimics natural myelin. Neutron reflectometry is an ideal method for studying the homogeneity and membrane stack properties of such samples due to the penetrative nature of neutrons as well as the possibility for contrast variation governed by the different scattering lenght densities of H and D. We want to uncover the very fundamental molecular details that underly the unique myelin ultrastructure, which helps us understand its genesis, stability and its molecular details in health and disease.
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RAASAKKA Arne; BARKER Robert; BAUMANN Anne; KURSULA Petri and LAULUMAA Saara. (2015). Membrane-stacking Properties of Myelin Proteins. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-745
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