Gregory R. Bowman, Ph.D.

Assistant Professor

Biochemistry and Molecular Biophysics

Lab Website
Publications (PubMed / NIH)

Office: 2915 South Building
Phone: 314-362-7433


The Bowman Lab seeks to understand the distribution of different structures a protein adopts and how this ensemble determines a proteins function. Examples of ongoing research projects include 1) understanding how mutations in the enzyme beta-lactamase change its specificity without changing the protein’s crystal structure, 2) designing allosteric drugs, and 3) developing algorithms for quickly building models of the different structures a protein adopts.

Select Publications

Porter J.R., Moeder K.E., Sibbald C.A., Zimmerman M.I., Hart K.M., Greenberg M.J., & Bowman G.R. (2019). “Cooperative Changes in Solvent Exposure Identify Cryptic Pockets, Switches, and Allosteric Coupling.” Biophys J. 2019 Mar 5;116(5):818-830. doi: 10.1016/j.bpj.2018.11.3144. Epub 2019 Jan 25. (Abstract)

Porter J.R., Zimmerman M.I., & Bowman G.R. (2019). “Enspara: Modeling molecular ensembles with scalable data structures and parallel computing.” J Chem Phys. 2019 Jan 28;150(4):044108. doi: 10.1063/1.5063794. (Abstract)

Knoverek C.R., Amarasinghe G.K., & Bowman G.R. (2018). “Advanced Methods for Accessing Protein Shape-Shifting Present New Therapeutic Opportunities.” Trends Biochem Sci. 2018 Dec 13. pii: S0968-0004(18)30248-2. doi: 10.1016/j.tibs.2018.11.007. [Epub ahead of print] (Abstract)

Zimmerman M.I., Porter J.R., Sun X., Silva R.R., & Bowman G.R. (2018). “Choice of Adaptive Sampling Strategy Impacts State Discovery, Transition Probabilities, and the Apparent Mechanism of Conformational Changes.” J Chem Theory Comput. 2018 Nov 13;14(11):5459-5475. doi: 10.1021/acs.jctc.8b00500. Epub 2018 Oct 23. (Abstract)

Sun X., Singh S., Blumer K.J., & Bowman G.R. (2018). “Simulation of spontaneous G protein activation reveals a new intermediate driving GDP unbinding.” Elife. 2018 Oct 5;7. pii: e38465. doi: 10.7554/eLife.38465. (Abstract)

Justin R Porter, Katelyn E Moeder, Carrie A Sibbald, Maxwell I Zimmerman, Kathryn M Hart, Michael J Greenberg, & Gregory R Bowman (2018). “Cooperative changes in solvent exposure identify cryptic pockets, conformational switches, and allosteric coupling” bioRxiv. September 18, 2018. (Abstract)

Su Z., Wu C., Shi L., Luthra P., Pintilie G.D., Johnson B., Porter J.R., Ge P., Chen M., Liu G., Frederick T.E., Binning J.M., Bowman G.R., Zhou Z.H., Basler C.F., Gross M.L., Leung D.W., Chiu W., & Amarasinghe G.K. (2018). “Electron Cryo-microscopy Structure of Ebola Virus Nucleoprotein Reveals a Mechanism for Nucleocapsid-like Assembly.” Cell. 2018 Feb 22;172(5):966-978.e12. doi: 10.1016/j.cell.2018.02.009. (Abstract)

Zimmerman M.I., Hart K.M., Sibbald C.A., Frederick T.E., Jimah J.R., Knoverek C.R., Tolia N.H., & Bowman G.R. (2017). “Prediction of New Stabilizing Mutations Based on Mechanistic Insights from Markov State Models.” ACS Cent Sci. 2017 Dec 27;3(12):1311-1321. doi: 10.1021/acscentsci.7b00465. Epub 2017 Nov 21. (Abstract)

Halstead A.M., Kapadia C.D., Bolzenius J., Chu C.E., Schriefer A., Wartman L.D., Bowman G.R., & Arora V.K. (2017). “Bladder-cancer-associated mutations in RXRA activate peroxisome proliferator-activated receptors to drive urothelial proliferation.” Elife. 2017 Nov 16;6. pii: e30862. doi: 10.7554/eLife.30862. (Abstract)

Niu H., Fujiwara H., di Martino O., Hadwiger G., Frederick T.E., Menéndez-Gutiérrez M.P., Ricote M., Bowman G.R., & Welch J.S. (2017). “Endogenous retinoid X receptor ligands in mouse hematopoietic cells.” Sci Signal. 2017 Oct 31;10(503). pii: eaan1011. doi: 10.1126/scisignal.aan1011. (Abstract)

Patrick G.J., Fang L., Schaefer J., Singh S., Bowman G.R., & Wencewicz T.A. (2017). “Mechanistic Basis for ATP-Dependent Inhibition of Glutamine Synthetase by Tabtoxinine-β-lactam.” Biochemistry. 2018 Jan 9;57(1):117-135. doi: 10.1021/acs.biochem.7b00838. Epub 2017 Oct 31. (Abstract)

Hart K.M., Moeder K.E., Ho C.M.W., Zimmerman M.I., Frederick T.E., & Bowman G.R. (2017). “Designing small molecules to target cryptic pockets yields both positive and negative allosteric modulators.” PLoS One. 2017 Jun 1;12(6):e0178678. doi: 10.1371/journal.pone.0178678. eCollection 2017. (Abstract)

Singh S. & Bowman G.R. (2017). “Quantifying Allosteric Communication via Both Concerted Structural Changes and Conformational Disorder with CARDS.” J Chem Theory Comput. 2017 Apr 11;13(4):1509-1517. doi: 10.1021/acs.jctc.6b01181. Epub 2017 Mar 22. (Abstract)

Sun X., Laroche G., Wang X., Ågren H., Bowman G.R., Giguère P.M., & Tu Y. (2017). “Propagation of the Allosteric Modulation Induced by Sodium in the δ-Opioid Receptor.” Chemistry. 2017 Apr 3;23(19):4615-4624. doi: 10.1002/chem.201605575. Epub 2017 Mar 20. (Abstract)

Brosey C.A., Ho C., Long W.Z., Singh S., Burnett K., Hura G.L., Nix J.C., Bowman G.R., Ellenberger T., & Tainer J.A. (2016). “Defining NADH-Driven Allostery Regulating Apoptosis-Inducing Factor” Structure. 2016 Dec 6;24(12):2067-2079. doi: 10.1016/j.str.2016.09.012. Epub 2016 Nov 3. (Abstract)