David Boehr

Professional Appointments and Affiliations

Associate Head for Undergraduate Education in Chemistry

Professor of Chemistry

Office 

107 Chemistry Building
University Park, PA 16802

Mailing Address

104 Chemistry Building

Education

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

Research

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

Mondal, S., G. Sarvari and D.D. Boehr. 2023. Picornavirus 3C proteins intervene in host cell processes through proteolysis and interactions with RNA. Viruses, 15, 2413. https://doi.org/10.3390/v15122413

Winston, D.S., S.D. Gorman and D.D. Boehr. 2022. Conformational transitions in yeast chorismate mutase important for allosteric regulation as identified by nuclear magnetic resonance spectroscopy. J. Mol. Biol., 434, 167531.   

Winston, D.S. and D.D. Boehr. 2021. The picornavirus precursor 3CD has different conformational dynamics compared to 3Cpro and 3Dpol in functionally relevant regions. Viruses, 13, 442. https://doi.org/10.3390/v13030442

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., 30, 543-557. https://doi.org/10.1002/pro.4011

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. https://doi.org/10.1021/acs.biochem.0c00277

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. https://doi.org/10.1074/jbc.RA119.010214