Probing membrane protein structure using neutron reflectivity
Membrane proteins represent about 30% of the proteomes of organisms and are dramatically under-represented in the structural database of the Protein Data Bank. This can be explained by their lack of stability and difficulty to crystallize. To answer this demand we propose to use a bacterial cell-free system to express hydrogenated and deuterated membrane proteins directly into a supported lipid bilayer in a neutron reflectivity (NR) solid-liquid cell. Cell-free systems are in vitro protein synthesis systems that use the extract (or lysate) from a prokaryotic or eukaryotic organism to provide the cellular machinery necessary for protein production. Here, we intend to use supported lipid bilayers to provide the lipidic environment into which the expressed membrane proteins will be directly inserted. To establish a proof of concept and demonstrate the potential of this new technique, we will investigate VDAC, a well characterized protein. Following these results, we will proceed to investigate the structure of Hepatitis C virus (HCV) proteins which have not, at this point, been crystallized.
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WATKINS Erik; MARTIN Donald and SORANZO Thomas. (2013). Probing membrane protein structure using neutron reflectivity. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-05-415