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DANIELLE C. LOHMAN 433 Babcock Dr. Madison, WI 53706-1544 (919) 349-3500 [email protected] EDUCATION PhD Integrated Program in Biochemistry, in progress University of Wisconsin at Madison GPA: 4.00 2012 – present Bachelor of Science in Chemistry, Biochemistry track Minor: Cognitive Science University of North Carolina at Chapel Hill GPA: 3.81 out of 4.00 2007 - 2011 TASSEP: Trans-Atlantic Science Student Exchange Program Université Paul Sabatier, Toulouse, France 2009 - 2010 RESEARCH EXPERIENCE Graduate Research Assistant Pagliarini Group (University of Wisconsin) 2012 - present The Pagliarini lab investigates the biochemical basis for mitochondrial dysfunction. Disruptions of normal mitochondria function are associated with human diseases including type II diabetes, Parkinson’s disease, and Alzheimer’s disease. Mitochondria are best known for their role in ATP production during oxidative phosphorylation. One essential component of the oxidative phosphorylation machinery is the electron transporter Coenzyme Q. My research focuses on understanding the enzymatic function and regulation of proteins involved in Coenzyme Q biosynthesis. Coenzyme Q is a lipophilic, redox active electron carrier required by the electron transport chain. Despite the importance of Coenzyme Q to human health, the pathway remains largely undefined and the biochemical regulation of Coenzyme Q biosynthesis is virtually unknown. Research into the biochemistry and regulation of proteins in this pathway will provide insight into mitochondrial disease associated with Coenzyme Q deficiency. Research Assistant Wolfenden Group (University of North Carolina) 2011 - 2012 My research in the Wolfenden lab focused on understanding the energetics of biological molecules and reactions. To appreciate and learn from nature’s catalysts, the Wolfenden lab studies the kinetics and thermodynamics of uncatalyzed enzymatic reactions. I was involved in three major projects, the first established a new standard for the most powerful biological catalyst: the S-O cleaving alkyl sulfatase. The second project involved understanding the stability of the S-N bond in alkyl sulfamates, whose cleavage is an important reaction in the degradation of heparin sulfate. My final project was a quantitative examination of the role desolvation plays in enzymatic catalysis, using the halide transferase reaction as a model. This work honed my analytical skills and trained me to understand and investigate the chemical context of biological processes. TECHNICAL SKILLS Instrumentation: 1H-NMR, Differential scanning fluorimetry, UV-visible spectrophotometry Chemical Techniques: preparation and purification of moisture sensitive compounds (sulfate monoesters), 17O-labeling experiments Kinetic Techniques: determination of chemical rate constants by method of initial rates under pseudo-first order conditions and analysis of kinetic data (Brønsted plot, pH rate profile, Eyring plot) Biochemical Techniques: radioactive labeling enzyme assays Molecular Biology Techniques: recombinant protein cloning, expression, and purification; standard E. coli & S. cerevisiae culturing GRANTS & AWARDS Biotechnology Training Program NIH Graduated with Highest Distinction UNC-CH 2012 - present May 2011 PUBLICATIONS Lohman, D. C.; Edwards, D. R.; Wolfenden, R. “Hydrolysis of N-alkyl Sulfamates and the Catalytic Efficiency of an S-N Cleaving Sulfamidase” J.O.C. 2012, 77, 2907-2910. Edwards, David R.; Lohman, D. C.; Wolfenden, R. “Catalytic proficiency: the extreme case of S-O cleaving sulfatases” J.A.C.S. 2012, 134, 525-531.