Highly hydrophobic proteins, including integral membrane proteins are of major interest for the scientific community due to their economical and biotechnological importance. Among them, a particular class is associated with the phospholipids monolayer of lipid bodies (LBs). These proteins share structural properties and are also connected to agronomic stakes (oleosins) or health issues (apolipoproteins and PAT proteins). Thanks to an heterologous expression system we developed in yeast, we are able to produce purified lipid bodies harboring these proteins and suitable for structural analysis. We will use this powerful tool to study the fold of hydrophobic integral protein in lipid bodies using SRCD-FTIR coupled approaches. This study will confirm our first results obtained in 2010 on AtS3 oleosin.