David D. Boehr

David D. Boehr

Main Content

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

Mailing Address:
104 Chemistry Building

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., X Liu, D.M. Musser, I.M. Moustafa, J.J. Arnold, C.E. Cameron and D.D. Boehr. 2017. Triphosphate reorientation of the incoming nucleotide as a fidelity checkpoint in viral RNA dependent RNA polymerases. J. Biol. Chem., 292, 3810-3826.

O’Rourke, K.F., A.M. Jelowiki and D.D. Boehr. 2016. Controlling active site loop dynamics in the (β/α)8 barrel enzyme indole-3-glycerol phosphate synthase. Catalysts, 6, 129.

Chan, Y.M., I.M. Moustafa, J.J. Arnold, C.E. Cameron and D.D. Boehr. 2016. Long-range communication between different functional sites in the picornaviral 3C protein. Structure, 24, 509-517.

Liu, X., D.M. Musser, C.A. Lee, X. Yang, J.J. Arnold, C.E. Cameron and D.D. Boehr. 2015. Nucleobase but not sugar fidelity is maintained in the Sabin I RNA-dependent RNA polymerase. Viruses, 7, 5571-5586.

Axe, J.M., E.M. Yezdimer, K.F. O’Rourke, N.E. Kerstetter, W. You, C.E. Chang and D.D. Boehr. 2014. Amino acid networks in a (β/α)8 barrel enzyme change during catalytic turnover. J. Am. Chem. Soc., 136, 6818-6821.

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

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

Biomolecular NMR spectroscopy

Biological

The role of protein structural dynamics in enzyme function and regulation

Physical

The role of protein structural dynamics in enzyme function and regulation

Spectroscopy

Biomolecular NMR spectroscopy

Chemical Biology

The biophysical chemistry of enzyme engineering