"Investigation of the Three-Dimensional Structure of Oleosin, a Membrane Protein"
Lipid droplets (LDs) are small organelles that serve as energy reservoirs for plants during seed growth and development. LDs are stabilized by oleosins, a membrane protein, which are hypothesized to adapt a “U” shape in the membrane. The mechanism by which oleosin is responsible for the stabilization of LDs is poorly understood due to the lack of structural characterization of oleosin. My research aims to deduce the three-dimensional shape (tertiary structure) of oleosin by measuring distances throughout the region of the protein inserted in the membrane. Förster Resonance Energy Transfer, molecular dynamic simulations, and alanine scanning are used to unveil the conformation of oleosin and to explore the turning region of oleosin to decipher the key residues in the folding of oleosin. The aim of this work is to gain insight into how the structure of oleosin is responsible for its ability to stabilize LDs and apply this knowledge to utilize LDs for purposes such as drug delivery.