David Boehr

Assistant Professor of Chemistry

240 Chemistry Building
University Park, PA 16802
Email: ddb12@psu.edu
(814) 863-8605

Web Sites:

Boehr Research Group

Education:

B.Sc., University of Lethbridge, Canada, 1993
Ph.D., McMaster University, Canada, 2004
Canadian Institutes of Health Research (CIHR), Postdoctoral Fellowship 2004-2007
Post-doc, The Scripps Research Institute, 2008

Honors and Awards:

NSERC of Canada Predoctoral Fellowship, 1998-2003

Selected Publications:

Boehr, D.D., McElheny, D., Dyson, H.J. and Wright, P.E. Millisecond fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands. Proc. Natl. Acad. Sci. USA. 2010, 107, 1373-1378.

Boehr, D.D., Nussinov, R. and Wright, P.E. The role of dynamic conformational ensembles in molecular recognition. Nat. Chem. Biol. 2009, 5, 789-796.

Boehr, D.D., McElheny, D., Dyson, H.J. and Wright, P.E. The dynamic energy landscape of dihyrofolate reductase catalysis. Science, 2006, 313, 1638-1642.

Boehr, D.D., Dyson, H.J and Wright, P.E. An NMR perspective on enzyme dynamics. Chem. Rev., 2006, 3055-3079.

Information:

The Boehr lab is interested in the role of protein dynamics in enzyme function, coordination and regulation. There is still controversy within the enzyme field concerning the importance of protein motion to enzyme function, which can impact practical applications of biochemistry like protein engineering and structure-based drug design. We believe a multi-disciplinary approach combining in vivo assays and biochemical/biophysical approaches, will be necessary to resolve the connections between enzyme activity, protein structure/dynamics and biological function. One of our main tools to analyze enzyme dynamics is nuclear magnetic resonance (NMR) that allows site-specific structural and dynamic detail across 10¹⁷ orders of magnitude (10^-12 - 10⁵ seconds). The Boehr lab combines NMR studies with more traditional enzyme techniques (e.g. steady-state enzyme kinetics, site-directed mutagenesis, protein folding, directed evolution) to elucidate the connections between enzyme function, structure and dynamics. We are currently focused on enzymes involved in viral and bacterial pathogenesis. We believe such studies guide us in making rational decisions regarding rational drug and/or vaccine design. These studies will also offer us more insight into the molecular evolution of protein function, structure and dynamics.

Research Interests:

Analytical: Protein Dynamics by High Field NMR
Biological: Protein Dynamics in Enzyme Function and Regulation
Physical: Protein Dynamics by High Field NMR
Bioanalytical
Biophysical
Spectroscopy
Bio Structure/Function
Enzymology

Departments:

Chemistry Undergraduate Academic Advisors: Advisor

Sections