The first member of the vanilloid sensing sub-family of transient receptor potential cation channels (TRPV1) is an ion channel located primarily in the nociceptive (pain-sensing) neurons of the peripheral nervous system. It is most strongly activated by high temperatures, protons, and capsaicin, the molecule responsible for the spice of hot chili peppers. From these examples of TRPV1 activators, it has been deduced that this ion channel plays a key role in the sensory transduction of pain that results from thermal burns, acid burns, and ingestion of noxious chemicals. Thus, the TRPV1 ion channel has potential to be a drug target for innovative pain medications and therapies. Before this is feasible, physiologically relevant details of TRPV1 structure and function must be elucidated. Expanding the understanding of how TRPV1 interacts and changes in various environments is also crucial. My research aims to determine if the lipid environment surrounding TRPV1 has significant impacts on its structural conformation. Electron resonance techniques such as EPR and DEER can be used to detect structural information of proteins; however, a number of steps precede this goal. First, I expressed and purifyied TRPV1 in large quantities. Next, I reconstituted the purified channel into vesicles. Vesicles are spheres of phospholipid bilayer and more accurately resemble the plasma membrane environment in which TRPV1 naturally occurs. Then electron resonance techniques were used to compare the structure of detergent-stabilized TRPV1 and TRPV1 reconstituted into vesicles. The comparison of TRPV1 structure in different lipid environments has a lot of implications in the applicability of structural studies conducted outside of physiologically relevant systems and for the future study of TRPV1.