Membrane Proteins (MPs) consist of about 1/3 of the proteome but the structural information available is very limited compared to that for soluble proteins. Despite this at least 60 % of all commercially available drugs are targeted at MPs. The insolubility of MPs in water has meant they have been more difficult to study than soluble proteins. One method of making them soluble in water while retaining functionality is to surround the hydrophobic section of the protein with an amphiphilic polymer, amphipol. Amphipols can be functionalised to bind to surfaces thereby tethering the MP to a platform. We (J-L. P) have achieved this and undertaken functional studies on such systems. We now aim to extend these studies to include the determination of the structural aspects of the immobilised MP layer and complexes. This will assist with optimisation of MP based device development.