We have a programme investigating the structure and function of protein scaffolds oriented on gold surfaces using sulfur chemistry for attachment. The aim is to direct the self-assembly of membrane protein arrays retaining the protein's three dimensional structure and native membrane orientation. Both of these aspects are crucial to the full functionality of a device. The geometry of the system is ideally suited to study by neutron reflection. The system is somewhat more complex than that typically formed by a peptide fragment or surfactant. In addition to the protein's complex shape there is also the insulating bilayer surrounding the protein that is crucial to functionality. Recent experiments at NIST have revealed that temperature is an important variable in the bilayer deposition. This proposal will investigate the impact of temperature on kinetics and the lipid layer structure.