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Omar Davulcu
Chemist

Dr. Omar Davulcu is a chemist with the Environmental Molecular Sciences Laboratory's Structural Biology Integrated Research Platform. He is currently working as a cryo-electron microscopist and biochemist at the Pacific Northwest Center for Cryo-EM in Portland, Oregon. Davulcu collaborates with researchers and users from both academia and industry to collect high-resolution electron microscopy data. He has been a structural biologist for more than 18 years and has experience in nuclear magnetic resonance, X-ray crystallography, and most recently, electron microscopy.

Research Interests

  • Electron Microscopy
  • Structural Biology

Education

  • PhD in Biochemistry, Florida State University
  • BS in Biochemistry, The University of Texas at Austin

Publications

2019

Meyer, N. L., G. Hu, O. Davulcu, Q. Xie, A. J. Noble, C. Yoshioka, D. S. Gingerich, A. Trzynka, L. David, S. M. Stagg, and M. S. Chapman. 2019. “Structure of the Gene Therapy Vector, Adeno-Associated Virus with Its Cell Receptor, AAVR.” eLife 8. https://doi.org/10.7554/eLife.44707.

2017

Davulcu, O., Y. Peng, R. Brüschweiler, J. J. Skalicky, and M. S. Chapman. 2017. “Elevated µs-ms Timescale Backbone Dynamics in the Transition State Analog Form of Arginine Kinase.” Journal of Structural Biology 200 (3): 258-266. doi.org/10.1016/j.jsb.2017.05.002.  

Peng, Y., A. L. Hansen, L. Bruschweiler-Li, O. Davulcu, J. J. Skalicky, M. S. Chapman, and R. Brüschweiler. 2017. “The Michaelis Complex of Arginine Kinase Samples the Transition State at a Frequency That Matches the Catalytic Rate.” Journal of the American Chemical Society 139 (13): 4846-4853. doi.org/10.1021/jacs.7b00236.  

Pillay, S., W. Zou, F. Cheng, A. S. Puschnik, N. L. Meyer, S. S. Ganaie, X. Deng, J. E. Wosen, O. Davulcu, Z. Yan, J. F. Engelhardt, K. E. Brown, M. S. Chapman, J. Qiu, and J. E. Carette. 2017. “Adenoassociated Virus (AAV) Serotypes Have Distinctive Interactions with Domains of the Cellular AAV Receptor.” Journal of Virology 91 (18). doi.org/10.1128/JVI.00391-17.  

Xie, Q., J. M. Spear, A. J. Noble, D. R. Sousa, N. L. Meyer, O. Davulcu, F. Zhang, R. J. Linhardt, S. M. Stagg, and M. S. Chapman. 2017. “The 2.8 Å Electron Microscopy Structure of Adeno-Associated Virus-DJ Bound by a Heparinoid Pentasaccharide.” Molecular Therapy - Methods and Clinical Development 5: 1-12. doi.org/10.1016/j.omtm.2017.02.004.  

2016

Godsey, M. H., O. Davulcu, J. C. Nix, J. J. Skalicky, R. P. Brüschweiler, and M. S. Chapman. 2016. “The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase.” Structure 24 (10): 1658-1667. https://doi.org/10.1016/j.str.2016.07.013.

Pillay, S., N. L. Meyer, A. S. Puschnik, O. Davulcu, J. Diep, Y. Ishikawa, L. T. Jae, J. E. Wosen, C. M. Nagamine, M. S. Chapman, and J. E. Carette. 2016. “An Essential Receptor for Adeno-Associated Virus Infection.” Nature 530 (7588): 108-112. doi.org/10.1038/nature16465.  

2015

Chapman, B. K., O. Davulcu, J. J. Skalicky, R. P. Brüschweiler, and M. S. Chapman. 2015. “Parsimony in Protein Conformational Change.” Structure 23 (7): 1190-1198. doi.org/10.1016/j.str.2015.05.011.  

2014

Davulcu, O., X. Niu, L. Brüschweiler-Li, R. Brüschweiler, J. J. Skalicky, and M. S. Chapman. 2014. “Backbone Resonance Assignments of the 42 kDa Enzyme Arginine Kinase in the Transition State Analogue Form.” Biomolecular NMR Assignments 8 (2): 335-338. doi.org/10.1007/s12104-013-9512-4.  

2013

Zhang, F., J. Aguilera, J. M. Beaudet, Q. Xie, T. F. Lerch, O. Davulcu, W. Colón, M. S. Chapman, and R. J. Linhardt. 2013. “Characterization of Interactions between Heparin/Glycosaminoglycan and Adeno-Associated Virus.” Biochemistry 52 (36): 6275-6285. doi.org/10.1021/bi4008676.  

2012

Clark, S. A., O. Davulcu, and M. S. Chapman. 2012. “Crystal Structures of Arginine Kinase in Complex with ADP, Nitrate, and Various Phosphagen Analogs.” Biochemical and Biophysical Research Communications 427 (1): 212-217. doi.org/10.1016/j.bbrc.2012.09.053.  

2011

Bush, D. J., O. Kirillova, S. A. Clark, O. Davulcu, F. Fabiola, Q. Xie, T. Somasundaram, W. R. Ellington, and M. S. Chapman. 2011. “The Structure of Lombricine Kinase: Implications for Phosphagen Kinase Conformational Changes.” Journal of Biological Chemistry 286 (11): 9338-9350. doi.org/10.1074/jbc.M110.202796.  

Davulcu, O., J. J. Skalicky, and M. S. Chapman. 2011. “Rate-Limiting Domain and Loop Motions in Arginine Kinase.” Biochemistry 50 (19): 4011-4018. doi.org/10.1021/bi101664u.  

Niu, X., L. Bruschweiler-Li, O. Davulcu, J. J. Skalicky, R. Brüschweiler, and M. S. Chapman. 2011. “Arginine Kinase: Joint Crystallographic and NMR RDC Analyses Link Substrate-Associated Motions to Intrinsic Flexibility.” Journal of Molecular Biology 405 (2): 479-496. doi.org/10.1016/j.jmb.2010.11.007.  

2009

Davulcu, O., P. F. Flynn, M. S. Chapman, and J. J. Skalicky. 2009. “Intrinsic Domain and Loop Dynamics Commensurate with Catalytic Turnover in an Induced-Fit Enzyme.” Structure 17 (10): 1356-1367. doi.org/10.1016/j.str.2009.08.014.  

2008

Hoffman, G. G., O. Davulcu, S. Sona, and W. R. Ellington. 2008. “Contributions to Catalysis and Potential Interactions of the Three Catalytic Domains in a Contiguous Trimeric Creatine Kinase.” FEBS Journal 275 (4): 646-654. doi.org/10.1111/j.1742-4658.2007.06226.x.  

2005

Davulcu, O., S. A. Clark, M. S. Chapman, and J. J. Skalicky. 2005. “Main Chain 1H, 13C, and 15N Resonance Assignments of the 42-kDa Enzyme Arginine Kinase.” Journal of Biomolecular NMR 32 (2): 178. doi.org/10.1007/s10858-005-6731-8. [Letter]