Membrane-stacking Properties of Myelin Proteins

DOI

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 continuation experiment at the D17 reflectometer, which is the best instrument for the plans at hand: we want to measure 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 length densities of H and D. We want to uncover the very fundamental molecular architecture that underly the unique myelin ultrastructure, which helps us understand its genesis, stability and its molecular details in health and disease.

Identifier
DOI https://doi.org/10.5291/ILL-DATA.8-02-767
Metadata Access https://data.ill.fr/openaire/oai?verb=GetRecord&metadataPrefix=oai_datacite&identifier=10.5291/ILL-DATA.8-02-767
Provenance
Creator Luchini, Alessandra; Baumann, Anne; Ulrich, Anne; Raasakka, Arne; Burck, Jochen; Barker, Robert
Publisher Institut Laue-Langevin
Publication Year 2017
Rights OpenAccess; info:eu-repo/semantics/openAccess
OpenAccess true
Representation
Resource Type Dataset
Size 3 GB
Version 1
Discipline Particles, Nuclei and Fields