Dystrophin is a rod shaped protein consisting of amino- and carboxy-terminal binding domains linked by a large central rod composed of 24... Show moreDystrophin is a rod shaped protein consisting of amino- and carboxy-terminal binding domains linked by a large central rod composed of 24 homologous copies of the STR motif and 5 non-homologous regions termed hinges. There are no high-resolution crystallographic structures available for the STR repeats. This work yielded protein crystals and data sets of two STR fragments (d5 & d16-17). Though unable to produce a high resolution structure, this work examines the physical properties of the rod region utilizing hydrophobic moment analysis and molecular dynamics to suggest flexibility among the helices of the STR fragments. Helical shifting appears to possibly occur among the more stable STR tandems to increase the cooperation among certain adjacent fragments. A full understanding of how these properties vary along the length of the rod has implications for the engineering of these rods regions in future dystrophin therapies. Ph.D. in Biology, July 2012 Show less
Query
(-) mods_name_creator_namePart_mt:"Reinfelds, Pauls Edvins"
