ii To my mom and dad, who gave me a thirst for knowledge and the desire to learn.iii Acknowledgements I would like to thank Dr. Linda Columbus for allowing me to work in her lab, study inclusion proteins, and pushing my limits.Thank you Columbus and Mura Lab members for all their technical assistance and feedback.Dr. John D. Shannon for his incredible patience and assistance with MALDI-TOF MS and circular dichroism.Many thanks to Jessica Sarver in the Cafiso lab for allowing me to think out loud about EPR.Thank you to Sandy, Vicki, and Kevin in Facilities Management who kept me laughing, updated me on the news and "goings on" in the department in the "wee" hours of the morning.Special thanks to Tsega Solomon who gave me invaluable technical advice, interesting philosophical debates over lunch, and a renewed interest in shopping. How I will miss you! Special thanks to Dr. Kim Bassett for her listening ear and unconditional friendship. demonstrated the hexa-histidine tag disrupted dimer formation; however, after cleavage of the tag with thrombin, dimer was reformed. Circular dichroism of the construct confirmed the dimer was all α-helical as expected for a SNARE motif. Finally, two single cysteine mutants were prepared and spin-labeled. Continuous wave electron paramagnetic resonance confirmed the sites were spin-labeled and the lineshapes were consistent with moderately immobilized spin labels expected for a tertiary contact. Future double electronelectron resonance experiments will measure the distance between the spin labels, which will elucidate the dimer orientation.