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David Boehr

Associate Professor of Chemistry
david boehr

Professional Appointments and Affiliations

Associate Head for Undergraduate Education in Chemistry

Associate Professor of Chemistry



107 Chemistry Building
University Park, PA 16802


Mailing Address

104 Chemistry Building



Postdoc, The Scripps Research Institute, 2008

Canadian Institutes of Health Research (CIHR), Postdoctoral Fellowship 2004-2007

Ph.D., McMaster University, Canada, 2004

B.Sc., University of Lethbridge, Canada, 1993


Honors and Awards

National Science Foundation CAREER Award, 2011

NSERC of Canada Predoctoral Fellowship, 1998-2003



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 1017orders 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.


Selected Publications

O'Rourke, K.F., R.N. D'Amico, D. Sahu and D.D. Boehr. 2020. Distinct conformational dynamics and allosteric networks in alpha tryptophan synthase during active catalysis. Protein Sci., in press.

Gorman, S.D., D.S. Winston, D. Sahu and D.D. Boehr. 2020. Different solvent and conformational entropy contributions to the allosteric activation and inhibition mechanisms of yeast chorismate mutase. Biochemistry, 59, 2528-2540.

Boehr, A.K., J.J. Arnold, H.S. Oh, C.E. Cameron and D.D. Boehr. 2019. 2'-C-methylated nucleotides terminate virus RNA synthesis by preventing active site closure of the viral RNA-dependent RNA polymerase. J. Biol. Chem., 294, 16897-16907.

Shi, J., J.M. Perryman, X. Yang, X. Liu, D.M. Musser, A.K. Boehr, I.M. Moustafa, J.J. Arnold, C.E. Cameron and D.D. Boehr. 2019. Rational control of poliovirus RNA-dependent RNA polymerase fidelity by modulating motif-D loop conformational dynamics. Biochemistry, 58, 3735-3743.

O'Rourke, K.F., D. Sahu, Y.K. Bosken, R.N. D'Amico, C.A. Chang and D.D. Boehr. 2019. Coordinated network changes across the catalytic cycle of alpha tryptophan synthase. Structure, 27, 1405-1415.

Gorman, S.D., R.N. D'Amico, D.S. Winston and D.D. Boehr. 2019. Engineering allostery into proteins. Adv. Exp. Med. Biol., 1163, 359-384.