The National Science Foundation’s Molecular and Cellular Biosciences Division recently honored Elizabeth E. Howell, a professor in the Department of Biochemistry and Cellular and Molecular Biology, by selecting one of her computer-generated models of a protein as a work of art showcasing the broad spectrum of science supported by NSF. Howell studies the structure and function of proteins and has worked extensively on the enzyme dihydrofolate reductase. Inhibitors of this enzyme are used to treat cancer as well as a number of bacterial infections and malaria. During the course of her studies, Howell has created detailed molecular models that show the three-dimensional structure of this protein and give a high resolution picture of the parts of the protein that demonstrate its unique reaction chemistry. These models resulted in the artwork that NSF is hanging at its headquarters in Arlington, Virginia, during the next year. The artwork has previously appeared on the cover of the Journal of Computationally Aided Molecular Design.
Yahashiri, A., Howell, E.E., Kohen, A. (2008), “Tuning of the H-Transfer Coordinate in Primitive versus Well-Evolved Enzymes,” ChemPhysChem 9: 980-982.
Chopra, S., Dooling, R., Horner, C.G., and Howell, E.E. (2008), “A Balancing Act: Net Uptake of Water During Dihydrofolate Binding and Net Release of Water upon NADPH Binding in R67 Dihydrofolate Reductase,” Journal of Biological Chemistry 283: 4690-4698.
Feng, J., Goswami, S. and Howell, E.E. (2008), “R67, the Other DHFR: Rational Design of an Alternate Active Site Configuration,” Biochemistry 47: 555-565.
Krahn, J.M., Jackson, M., DeRose, E.F., Howell, E.E. and London, R.E. (2007), “Structure of a Type II Dihydrofolate Reductase Catalytic Complex,” Biochemistry 46: 14878-14888.
Jackson, M.R., Beahm, R., Duvvuru, S., Narasimhan, C., Wu, J., Wang, H.-N., Hinde, R. J. and Howell, E.E. (2007), “A Preference for Edgewise Anion-Quadrupole Interactions between Aromatic and Carboxylate Amino Acids,” Journal of Physical Chemistry B 111, 8242-8249.