Tropomyosin, a muscle contractile protein, is destabilized when a destabilizing peptide, anti tropomyosin (anti-TM), inserts itself into the its coil coiled configuration and inhibits the two strands of the protein from binding tightly to each other. Biochemical and biophysical literature has linked the destabilization of tropomyosin to cardiomyopathy but studying the affects of the destabilized region also has potential to give us insight into other muscle related diseases including but not limited to muscular dystrophy and sarcopenia. It has been hypothesized that destabilization has resulted in the increase of the region's sensitivity to calcium and consequently, an increase in its contractions. The experimental process of this project comprises of the fluorescent tagging of the destabilizer peptide, the purification of the fluorescently labeled regions on the peptide, and the investigation of the binding behavior when incubated with myofibril. Analysis of the expected binding region exploits fluorescence microscopy which demonstrates the binding specificity of the peptide.