A solid supported, biomimetic lipid bilayer was formed on a gold substrate by adsorbing lipid vesicles on a self-assembled monolayer (SAM) consisting of thiol-lipopeptides mixed with thiol-peptides. The membrane was bound to the surface by the thiol-lipopeptides, the thiol-peptides being used to change the surface concentration of thiol-lipopeptide and hence control membrane fluidity. The lipid bilayer was formed by fusion of L-@alpha@-Phoshatidylcholine (eggPC) liposomes onto the mixed thiol-lipopeptide / thiol-peptide SAM. The free lipids replenish the tethered lipid layer and also form the second layer to complete the bilayer. A functionalized lipid bilayer was formed by incorporating H@super +@-ATP-synthase (extracted and purified from spinach chloroplastes) with the eggPC. This enzyme is a membrane integral protein that can synthesize or hydrolyze adenosine triphosphate (ATP) from or to adenosine diphosphate (ADP) and in doing so pumps H@super +@ through the bilayer. Impedance spectroscopy measurements demonstrated that the enzyme had not lost its biological functionality and was still active. The formation of the lipid bilayer was detected by using surface plasmon resonance spectroscopy (SPS). Finally Annexin V, a pore forming protein, was immobilised on a lipid bilayer by using Ca@super 2+@-ions to bind (by chelation) the negatively charged parts of the protein to the negatively charged lipids (1,2-Dimyristoyl-sn-Glycero-3-Phoshatidylserin) in the bilayer. Annexin V as a non-integral protein and its function as a passive ion transporter through the lipid bilayer was used for comparison of the active ion transporter H@super +@-ATP-synthase. The same techniques as described above were used to observe the formation and activity of this system.