Download Danielle C. Lohman - Biotechnology Training Program

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
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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
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Biotechnology Training Program NIH
Graduated with Highest Distinction UNC-CH
2012 - present
May 2011
PUBLICATIONS
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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.
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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.