David GravesProfessor Emeritus


Teaching Interests: Research Methods in Chemistry and Biochemistry, Concepts in Biochemistry, Advanced Biochemistry, Biophysical Chemistry, Biochemistry Laboratory

Office Hours: By appointment

  • BS, University of Alabama at Birmingham, Chemistry
  • PhD, University of Alabama at Birmingham, Biochemistry and Molecular Biology
  • Postdoctoral, University of Rochester

Following his postdoctoral fellowship at the University of Rochester, Dr. Graves joined the faculty in the Department of Chemistry and Biochemistry at the University of Mississippi in 1984. He rose through the ranks of assistant, associate, and full professor at the University of Mississippi and was awarded the title of Distinguished Faculty Fellow from the University of Mississippi College of Liberal Arts in 2001. In 2003, Dr. Graves was recruited to become the chair of the Department of Chemistry at the University of Alabama at Birmingham. He served as chair of the department from May 2003 to July 2015.

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The focus of my research involves the biophysical characterization of nucleic acid structures and stabilities as related to both base sequence effects as well as complex formation with small molecules and proteins. My initial research efforts focused on DNA as a target for small molecules such as anticancer agents including intercalating and groove binders and the mechanistic processes of molecular recognition. An understanding of the forces that govern DNA base sequence-specific interactions for small molecules and/or proteins is fundamental towards our comprehension of basic processes associated with gene expression such as transcription, recombination, DNA repair, as well as the recognition of DNA cleavage sites for nuclear enzymes such as topoisomerase I and topoisomerase II.

More recently, our research has focused on the structural, stability, and protein-binding properties of G-quadruplex DNA fragments. Recent studies in my laboratory have demonstrated that small deoxyribonucleotides can act as modulators of a number of toll-like receptor (TLR) mediated biological responses, including cancer cell invasion. Although the nature of the TLR9-mediated cell invasion is not understood, the key determinant seems to reside in the stable nuclease-resistant structure(s) of the oligonucleotides either for binding to the target protein or protection from nuclease invasion. We continue to use a multifaceted approach of calorimetry and high-resolution NMR to discern the structure and stability of nucleic acids and protein-nucleic acid complexes.
  • CH 201: Research Methods in Chemistry and Biochemistry
  • CH 463, 763: Biophysical Chemistry
  • CH 461, 761: Advanced Biochemistry
  • CH 464, 764: Biochemistry Laboratory
  • CH 763: Physical Biochemistry
  • Beck, R.A.; Carter, P.; Shonsey, E.; Graves, D.E. Tandem DART-MS Methods for Methadone Analysis in Unprocessed Urine. Journal of Analytical Toxicology (in press, October, 2015).
  • Sandholm, J.; Tuomela, J.; Kauppila, J.H.; Harris, K.W.; Graves, D.E.; Selander, K.S. Hypoxia Regulates Toll-like Receptor 9 Expression and Invasive Function in Human Brain Cancer Cells In Vitro. Oncology Letters.(2014) 8, 266-274.
  • Hudson, J.S.; Ding, L.; Le, V.; Lewis, E.; Graves, D.E. Recognition and Binding of Human Telomeric G-Quadruplex DNA by Unfolding Protein 1 (UP1). Biochemistry. 2014, 53 (20), 3347-3356.
  • Hayden, K. L.; Graves, D.E. Addition of bases to the 5’-end of hyman telomeric DNA:  Influences on thermal stability and energetics of unfolding. Molecules2014, 19, 2286-2298.
  • Kauppila, J.H.; Karttunen, T.J.; Saarnio, J.; Nyberg, P.; Salo, T.; Graves, D.E.; Lehenkari, P.P.; Selander, K.S. Short DNA Sequences and Bacterial DNA Induce Esophageal, Gastric, and Colorectal Cancer Cell Invasion. Acta Pathologica Microbiologica et Immunologica Scandinavica2013, 121 (6), 511-522.
  • Tuomela, J.; Sandholm, J.; Kaakinen, M.; Patel, A.; Kauppila, J.H.; Ilvesaro, J.; Chen, D.; Harris, K.W.; Graves, D.E.; Selander, K.S. DNA from dead cancer cells induce TLR9-mediated invasion and inflammation in living cancer cells. Breast Cancer Res. Treat.2013, 142(3), 477-487.
  • Ketron, A.C.; Denny, W.A.; Graves, D.E.; Osheroff, N. Amsacrine as a Topoisomerase II Poison:  Importance of Drug-DNA Interactions. Biochemistry2012, 51(8), 1730-1739.
  • Aldred, K.J.; McPherson, S.A.; Wang, P.; Kerns, R.J.; Graves, D.E.; Turnbough, C.L.; Osheroff, N. Drug Interactions with Bacillus Anthracis Topoisomerase IV:  Biochemical Basis for Quinolone Action and Resistance. Biochemistry. 2012, 51(1), 370-381.
  • Pitts, S.; Jablonsky, M.; Duca, M.; Dauzonne, D.; Monneret, C.; Arimondo, P.; Anklin, C.; Graves, D.E.; Osheroff, N. Contributions of the D-Ring to the Activity of Etoposide Against Human Topoisomerase II: Potential Interactions with DNA in the Ternary Enzyme-Drug-DNA Complex. Biochemistry2011, 50(22), 5058-5066.
  • Gentry, A.C.; Pitts, S.L.; Jablonsky, M.J.; Bailly, C.; Graves, D.E.; Osheroff, N. Interactions between the Etoposide Derivative F14512 and Human Type II Topoisomerases: Implications for the C4 Spermine Moiety in Promoting Enzyme-Mediated DNA Cleavage. Biochemistry2011, 50 (15), 3240-3249.
  • American Chemical Society (1980-present)
  • American Association for Cancer Research (1988-present)
  • American Association for the Advancement of Science (1982-present)
  • Biophysical Society (1984-present)
  • Sigma Xi (1984-present)
  • Federation of American Society for Experimental Biology (1985-present)
  • Federation of American Society for Biochemistry and Molecular Biology (1986-present)
  • Student Affiliate of the American Chemical Society — UAB Chapter
  • Southeastern Undergraduate Research Conference  (SURC)