This study aims to better understand and verify the molecular interaction between enolase and arrestin, which, beyond the scope of this research project, could eventually be incorporated into an eye therapy study. A molecular model has been developed that identified seven charged areas where arrestin and enolase directly interact with one another. To verify this model, site-directed mutagenesis will be used to reverse the charges in the areas of enolase that binds specifically to arrestin, which will induce multiple-binding disruptions. By purifying the mutated enolase protein containing the seven reversal charges, a fluorescence resonance energy transfer will be completed to verify, not only the binding disruptions, but also the overall molecular model itself.