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Drug resistance to the current treatments on the market is on the rise, therefore there is strong interest in understanding what could be causing the resistance, how resistance could be spreading through the population, and finding some possible new drug targets. One protein of interest is Radiation Sensitive Protein 51 (Rad51). It is a protein that is involved in homologous recombination as well as other processes such as DNA damage repair. While Trichomonas vaginalis traditionally has been known to replicate via binary fission, a modified form of closed mitosis, there is some evidence that meiosis, or at least some form of genetic recombination, could occur in the organisms, possibly contributing to the resistance. The focus of my project was gaining an understanding of how the Trichomonas vaginalis Rad51 protein (TvRad51) could, either directly or indirectly, play a role in generating diversity that could lead to resistance. Since functional assays of purified Rad51 protein were previously unsuccessful, this study attempted to investigate TvRad51’s ability to interact with known binding partners via protein-protein interactions, while exploring new targets using yeast two-hybrid. Localization of TvRad51 showed that it behaves differently than the human version giving more information to understand how TvRad51 functions. Lastly, preliminary studies were conducted to evaluate the potential role of TvRad51 in telomere maintenance.