Pederson, CaitlinSchneider, KatieCembran, Alessandro2018-08-292018-08-292016https://hdl.handle.net/11299/199848University Honors Capstone Project Paper and Poster and Undergraduate Research Opportunities Program (UROP), University of Minnesota Duluth, 2016. Department of Chemistry and Biochemistry. Caitlin Pederson authored paper and poster; Katie Schneider and Alessandro Cembran authored poster.Dystrophin is a cytoplasmic protein and it is an integral part of the protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix. Mutations in dystrophin are responsible for muscular dystrophy, and an understanding of dystrophin’s mechanism of function is the first step towards the development of therapies. Twenty four spectrinrepeat (SR) domains constitute the bulk of dystrophin, and the goal of this research was to test whether coupling multiple repeats affects the force required to unfold them under mechanical stress. To this end, we investigated with molecular dynamics simulations the structure, dynamics, and response to mechanical stress of the repeat SR-17 and of the dimer SR-17:18.enSwenson College of Science and EngineeringUniversity of Minnesota DuluthUniversity HonorsUndergraduate Research Opportunities ProgramDepartment of Chemistry and BiochemistryScholarly Text or Essay