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Eberly College of Science Department of Chemistry
David Boehr

David Boehr

Main Content

  • Assistant Professor of Chemistry
Office:
107 Chemistry Building
University Park, PA 16802
Email:
(814) 863-8605

Education:

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

Honors and Awards:

  1. National Science Foundation CAREER Award, 2011
  2. NSERC of Canada Predoctoral Fellowship, 1998-2003

Selected Publications:

Yang, X., E.D. Smidansky, K.R. Maksimchuk, D. Lum, J.L. Welch, J.J. Arnold, C.E. Cameron and D.D. Boehr, Motif D or viral RNA-dependent RNA polymerases determines efficiency and fidelity of nucleotide addition. Structure, 2012, 20, 1519-1527.

Weikl, T.R. and D.D. Boehr, Conformational selection and induced changes along the catalytic cycle of Escherichia.coli dihydrofolate reductase. Proteins, 2012, 80, 2369-2383.

Zaccardi, M.J., O. Mannweiler and D.D. Boehr, Differences in the catalytic mechanisms of mesophilic and thermophilic indole-3-clycerol phosphate synthase enzymes at their adaptive temperatures. Biochem. Biophys. Res. Commun., 2012, 418, 324-329.

Boehr, D.D. Promiscuity in protein-RNA interactions: Conformational ensembles facilitate molecular recognition in the spliceosome: Conformation diversity in U2AF(65) facilitates binding to diverse RNA sequences. Biosessays, 2012, 34, 174-180. 

Yang, X., J.L. Welch, J.J. Arnold and D.D. Boehr, Long-range interaction networks in the function and fidelity of poliovirus RNA-dependent RNA polymerase studied by nuclear magnetic resonance. Biochemistry, 2010, 49, 9361-9371.

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

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