Abstract
The myelin sheath is a unique membrane, tightly wrapped around selected axons in the vertebrate nervous system. The multilayered myelin proteolipid membrane contains a specific set of proteins, many of which share no homology with other known proteins. We are interested in the structure, function, interactions, and dynamics of myelin proteins and use multidisciplinary methods to study these relationships. We have solved crystal structures of myelin-specific proteins, characterized their membrane-binding properties, and initiated experiments to pinpoint details of protein dynamics. Among our most recent results are a comprehensive X-ray crystal structure-based characterization of the reaction cycle of the myelin enzyme CNPase, the identification of several myelin-specific proteins as intrinsically disordered molecules, and the analysis of molecular dynamics in myelin proteins and the lipid bilayers they interact with by neutron scattering. All the results will be important in understanding the formation of the myelin membrane multilayer, as well as the roles the myelin proteins play in myelination and myelin-related diseases.
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