Tropomyosin, an elongated two stranded helical protein found in the cytoskeleton, is one of the proteins that are involved in the contraction of muscles. In a muscle's relaxed state, the tropomyosin-troponin complex prevents the myosin head from binding productively to actin. However, when calcium binds to troponin C, it causes a structural change that enables the myosin head to form a crossbridge that induces muscle contraction. An anti-tropomyosin peptide (anti-TM), was rationally designed to destabilize the tropomyosin coiled coil where a high frequency of hypertrophic cardiomyopathy mutations occur. Computational simulations suggest that these hypertrophic cardiomyopathy mutations destabilize the coiled coil structure in this region. One hypothesis is that the destabilization of tropomyosin in this region might impact calcium ion sensitivity and increased muscle contraction. The experimental process of this project comprises the fluorescent tagging of the peptide, the purification of the fluorescently labeled peptide, and the investigation of its binding to tropomyosin in myofibrils. These studies demonstrate the ability to design anti-TM peptides that will target specific regions of the tropomyosin molecule with the potential to be used as a tool to dissect the functional characteristics of different regions of the tropomyosin molecule.