Dr. Gloria E.O. Borgstahl is a Professor at the Eppley Institute for Research in Cancer & Allied Diseases, University of Nebraska Medical Center. She grew up in Dubuque, Iowa, the youngest of seven and a first-generation scientist. She graduated with her BSE in Biomedical Engineering and a PhD in Biochemistry at the University of Iowa. She performs structural biology research on the protein-DNA and protein-protein interactions that govern DNA metabolic processes. Her current studies include an examination of the effects of posttranslational modification on protein-protein protein-DNA complexes, their binding and DNA repair activity. The laboratory is also using high throughput screening techniques to find small molecule inhibitors of protein-protein interactions as potential breast, ovarian and pancreatic cancer treatments. A second major focus is on neutron crystallography of human manganese superoxide dismutase (MnSOD) which included a NASA project involving crystal growth at the International Space Station. Neutron crystallography has revealed the all-atom structure of MnSOD in oxidized and reduced resting states as well as the product inhibited complex. Data reveal how proximity to the active site metal dramatically affect amino acid pKas and these unusual pKas are essential to the enzymes concerted proton electron transfer (PCET) mechanism for the dismutation of superoxide to hydrogen peroxide and oxygen.
Dr. Gloria E.O. Borgstahl is a Professor at the Eppley Institute for Research in Cancer & Allied Diseases, University of Nebraska Medical Center. She grew up in Dubuque, Iowa, the youngest of seven and a first-generation scientist. She graduated with her BSE in Biomedical Engineering and a PhD in Biochemistry at the University of Iowa. She performs structural biology research on the protein-DNA and protein-protein interactions that govern DNA metabolic processes. Her current studies include an examination of the effects of posttranslational modification on protein-protein protein-DNA complexes, their binding and DNA repair activity. The laboratory is also using high throughput screening techniques to find small molecule inhibitors of protein-protein interactions as potential breast, ovarian and pancreatic cancer treatments. A second major focus is on neutron crystallography of human manganese superoxide dismutase (MnSOD) which included a NASA project involving crystal growth at the International Space Station. Neutron crystallography has revealed the all-atom structure of MnSOD in oxidized and reduced resting states as well as the product inhibited complex. Data reveal how proximity to the active site metal dramatically affect amino acid pKas and these unusual pKas are essential to the enzymes concerted proton electron transfer (PCET) mechanism for the dismutation of superoxide to hydrogen peroxide and oxygen.