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Introduction: Members of the Ras protein family are involved in sending signals through the human body to regulate processes including cell growth. Acting as a molecular switch, Ras alternates between its active and inactive states (“on” and “off”) depending on its binding to either GTP or GDP. Upon the introduction of a mutation, Ras becomes incapable of performing the GTP hydrolysis reaction at a controlled rate. This results in the protein remaining in the “on” state for prolonged periods of time, disturbing its role in the regulation of cell growth and causing tumors to form. In the genome of cancerous tumors, mutations that permanently activate Ras have been observed and analyzed at three distinct locations, one being Q61. Previous research1 shows how the Q61 residue contributes to the protein’s function by stabilizing the water molecule in the active site, but little research has been done studying the Y32 residue, which has also been implicated in the mechanism. This research investigates the role Y32 plays in activating Ras via introduction of a different amino acid and measurement of the mutated protein’s activity in the hydrolysis of GTP.