Conformational analysis of membrane proteins in magnetically oriented bicelles

Membrane proteins are notoriously refractive to structural and conformational characterisation. We propose the development of a SANS-based approach for conformational analysis of membrane proteins, in which we study a membrane protein, bacteriorhodopsin, embedded within magnetically oriented membrane-mimicking bicellar systems. We propose to produce perdeuterated recombinant bacteriorhodopsin within an E. coli host and reconstitute the purified protein into protonated bicellar systems of DMPC and DHPC. In the presence of lanthanide ions, such proteobicelles will be aligned with bilayer normal along an external magnetic field. We aim to validate the approach and obtain the characteristic dimensions of a typical 7TMD bundle using SANS on ZOOM.