Pascolutti R., Sun X., Kao J., Maute R., Ring A.M., Bowman G.R., & Kruse A.C. (2016). “Structure and Dynamics of PD-L1 and an Ultra High-Affinity PD-1 Receptor Mutant.” Structure. 2016 Oct 4;24(10):1719-1728. doi: 10.1016/j.str.2016.06.026. Epub 2016 Sep 8. (Abstract)
Bowman G.R.
Accurately modeling nanosecond protein dynamics requires at least microseconds of simulation.
J Comput Chem. 37(6):558-66. (2016) (Abstract)
Zimmerman, M.I. and Bowman, G.R.
FAST Conformational Searches by Balancing Exploration/Exploitation Trade-Offs
J. Chem. Theory Comput. 11:5747-5757 (2015). (Abstract)
Bowman, G.R.
Accurately modeling nanosecond protein dynamics requires at least microseconds of simulation.
J Comput Chem 37:558-566 (2016) (Abstract)
DuBay, K.H., Bowman, G.R. and Geissler, P.L.
Fluctuations within Folded Proteins: Implications for Thermodynamic and Allosteric Regulation
Acc. Chem. Res. 48:1098-1105 (2015). (Abstract)
Bowman, G.R. Bolin, E.R., Hart, K.M., Maguire, B.C. and Marqusee, S.
Discovery of multiple hidden allosteric sites by combining Markov state models and experiments
PNAS 112:2734-2739 (2015). (Abstract)
Bowman, G.R. and Geissler, P.L.
Extensive Conformational Heterogeneity within Protein Cores
J Phys Chem B 118:6417-6423.(2014). (Abstract)
Kohlhoff, K.J., Shukla, D., Lawrenz, M., Bowman, G.R., Konerding, D.E., Belov, D., Altman, R.B. and Pande, V.S.
Cloud-based simulations on Google Exacycle reveal ligand modulation of GPCR activation pathways
Nature Chemistry 6:15-21 (2014). (Abstract)
Qiao, Q., Bowman G.R., Huang X.
Dynamics of an Intrinsically Disordered Protein Reveal Metastable Conformations That Potentially Seed Aggregation
J Am Chem Soc 135:16092-16101. (2013). (Abstract)
Bowman, G.R., Meng, L. and Huang, X.
Quantitative comparison of alternative methods for coarse-graining biological networks
J Chem Phys 139:121905. (2013). (Abstract)