Abstract: Peroxisome proliferator-activated receptor-gamma (PPAR-g) is a key drug target for the regulation of Type II Diabetes (T2D) due to its role in mediating the levels of glucose in the bloodstream. Currently, the relationship between the conformational states of PPARg, which are influenced by ligand binding, are relatively unstudied and could be very influential in determining ligand binding type and functional state. By determining the conformational states adopted by PPARg with and without ligand presence, we can better assess the landscape of structures adopted by PPARg, which can influence future drug design. Molecular dynamics (MD) simulations were used to simulate the apo, active, inactive, unbound, and bound structures of PPARg to compare local and global structural changes. Of particular interest is the state of Helix 12 (H12), which undergoes the most significant conformational change in the presence of a ligand and is, therefore, one of the first indicators of the active or inactive state of PPARg. Ligand presence influences H12 to remain or move into the active position. In the absence of a ligand, H12 oscillates freely between the active and inactive position. Our initial results allowed us to see minor distinctions between the test systems. Further research includes identifying key binding residues that affect this conformational oscillation and quantify the movement of H12 between the active and inactive position. A deeper understanding of the conformational states adopted by PPARg would allow for a more robust model of novel drug interaction.