While at Notre Dame her research focus was on plasminogen, the zymogen, that when converted into its active form, plasmin, is able to activate the fibrinolytic system resulting in the degradation of fibrin and extracellular matrices. Group AStreptococcus (GAS) is able to hijack this system leading to a more invasive infection. This process is mediated by proteins found on the surface of the bacteria. One such protein is PAM that binds specifically to one of the lysine binding sites within the kringle domains of plasminogen. My interests are to further understand the role of the lysine binding sites in PAM binding.
Dr. Beck is currently working for Dr. Robert Stahelin, Retter Professor of Pharmacy, Professor of Medicinal Chemistry and Molecular Pharmacology at Purdue University, West Lafayette, Indiana. Her post doctorate research centers on studying VP40 oligomerization and confirmation.