Development and characterization of a polymerization deficient actin monomer and longitudinal actin dimer
Actin, along with a myriad of actin binding proteins such as myosin, is involved in a number of cellular processes in both muscle and non-muscle cells. The acquisition of an atomic resolution structure of filamentous actin (F-actin) is essential in order to gain an in-depth understanding of actin dynamics. Since actin polymerizes to varying lengths, determining the crystal structure of F-actin requires the generation of short polymerization-deficient F-actin oligomers. Due to its role in muscle contraction, elucidating the crystal structure of the acto-myosin complex is of particular interest to researchers. This thesis describes the characterization of polymerization-incompetent actin monomers, as well as the development of a longitudinal actin dimer that is both polymerization deficient and is able to bind myosin.