The project I was working on for the past year was the titled “ The effects of Rabbit Amino Acid Mutation on the Human Prion Protein”. For this project I used computer simulations to analyze the effects of mutating a specific amino acid in the human prion protein to the rabbit variant. That amino acid is at residue 255, the tyrosine was mutated to an alanine. The human prion protein is capable of causing several deadly diseases when it misfolds. When the protein misfolds it has a propensity to aggregate. Diseases that can be caused by the misfolded prion protein are transmissible spongiform encephalitis, Creutzfeldt-Jakob disease, chronic fatal insomnia and kuru. Prion diseases can occur in several species however, there are a few notable species that have prion variants are resistant to misfolding. Some of these are dogs, horses, and rabbits. Understanding which differences prevent human prion protein from misfolding could lead to better treatment for prion diseases. Our hypothesis is that the mutation is more stable so it will have a higher free energy barrier to induce conformational changes. This project is a part of Dr. Fernandez-Funez’s research on the Human Prion protein. This particular variant is one of the variants his lab was researching so analyzing the variant with computer simulations would aid in our understanding of the experimental results.