Membrane proteins (MPs) continue being an elusive target for research due to the challenges regarding isolation and preservation of their native states. These problems can be overcome by immobilizing MPs in so-called nanodics, which can be perceived as stabilized pathces of lipids. In our experiment proposal we seek to clarify the exact binding position of UDP-gluosyltransferase that participates in a metabolon comprised of multiple enzymes of the cytochrome P450 (CYP) superfamily in Sorghum Bicolor: cytochrome P450 reductase (CPR) and two cytochromes P450, CYP79A1 and CYP71E1. UGT85B1 is believed to bind to CYP71E1, hence the key element in our proposal is to investigate whether and where the UGT85B1 displays affinity. Furthermore, the effect of lipid phase is to be examined by varying temperature from 15 to 30 degrees celsius. In total, the overall strategy revolves around CPR, CYP79A1 and CYP71E1 captured in nanodics and utilizing neutron reflectometry to detect changes in the density of the different sublayers in the adsorbed layer.