Seeds need fuel to germinate and grow into plants. They get this fuel from oil bodies. Oil bodies are micelles that package hydrophobic triacylglycerides (TAGs) or “fat” within seeds. The outer membrane of oil bodies contains a monolayer of phospholipids and several proteins, the most abundant being oleosins. Oleosins structure is unknown, however the amino acid sequence suggests there are three domains. The Hydrophilic domains are the N- and C-terminal domains which are thought to sit atop the phospholipid heads. The final domain is a central hydrophobic domain that is thought to insert into the membrane anchoring the protein. The hydrophobic domain contains a highly preserved proline knot motif that creates a hairpin turn and sends the other end of the protein back through the membrane. Despite the understanding of the localisation and primary structure of oleosins the function and secondary structure are a mystery. I discovered a conserved charged region on the C-terminal domain and hypothesised this region was essential for interactions occurring for oleosin function. Using transient expression via agroinfiltration I have investigated the function of this region of oleosins and discovered how the interactions oleosin makes with other oleosins and other proteins in the cytoplasm to carry out its function.