Familial hypertrophic cardiomyopathy (FHC) is a pathological thickening of the muscles surrounding the heart resulting in a reduction in chamber volume and a subsequent failure to fill and eject blood properly. This failure to pump and supply blood to the body’s peripheral organs can lead to shortness of breath, chest pain, tissue ischemia and in some extreme cases, sudden cardiac death. My current research is focused on analyzing and characterizing mutant myosin molecules that have been linked to cases involving FHC, and determining the link between the molecular disfunction of the mutant and its subsequent phenotype in patients. My primary technique of investigation is the in vitro motility assay.
Tropomyosin is an actin-binding protein that functions to regulate muscle contraction in cardiac and skeletal muscle. In low calcium environments, tropomyosin prevents contraction by blocking the myosin binding site on actin, while elevated calcium concentrations cause tropomyosin’s position on actin to shift resulting in myosin binding and muscle contraction. The precise method and timescale of tropomyosin binding to actin remains a mystery. I am currently working on a method to visualize fluorescently labeled tropomyosin molecules as they search for their binding sites on actin in real-time. My primary techniques of investigation are the in vitro motility assay and TIRF microscopy.
Stevens Institute of Technology
Hoboken, NJ from Sep. 2003- May 2007
Major – Chemical Biology
Minor – ChemistryBoston University School of Medicine
3rd year Ph.D. Candidate