Terry J. Watt, Ph.D.
Assistant Professor

Telephone Number: 504-520-5271
Room Number: NCF - Room 314
Email Address:



Introduction to Biochemistry (3130), Introduction to Biochemistry Lab (3130L), Genomics & Proteomics Lab (4150L), General Chemistry II Lab (1021L)


Short Professional Biography

Dr. Watt earned a B.S. in technical writing prior to completing a dual B.S./M.S. program in chemistry at Carnegie Mellon University.  His M.S. thesis, under the guidance of Dr. Bruce Armitage, described the synthesis of cyanine dyes and their nucleic acid binding properties.  In 2007, Dr. Watt earned a Ph.D. from the School of Chemistry and Biochemistry at the Georgia Institute of Technology.  His dissertation research, with Dr. Donald Doyle, examined how engineered mutations in nuclear receptors influence protein-ligand binding affinity and specificity, the self-association of the receptors, protein stability, and the overall intracellular activity of the proteins.  Dr. Watt then moved to the University of Michigan in Ann Arbor as a postdoctoral research associate in the lab of Dr. Carol Fierke.  His work there included assaying metal-dependent small molecule fluorescence, disrupting cellular metal homeostasis with toxic metals, analyzing the substrates of enzymes involved in post-translational modifications, and teaching undergraduate physical chemistry.  In 2010, Dr. Watt moved to Xavier University of Louisiana as a faculty member in the Department of Chemistry.


Research Interest

Dr. Watt's research activities focus on molecular recognition in biochemical systems.  He is currently researching how a small number of lysine deacetylases (KDACs, also known as histone deacetylases or HDACs) distinguish between the thousands of intracellular proteins that could serve as reaction substrates.  Acetylation of lysine is one of the most common post-translation modifications of proteins, and the acetylation/deacetylation cycle has central roles in gene expression, regulation of intracellular processes, and development of cancers.  To characterize KDAC substrate binding, Dr. Watt uses spectroscopy, enzyme kinetics, molecular biology, statistical models, and molecular modeling.


Current Grant Support

“Molecular characteristics of lysine deacetylase interactions.”  Department of Defense HBCU/MI W911NF-13-1-0129.  PI.  01 May 2013 - 30 April 2016.


Recent Publications

Johanson, K. E.; Watt, T. J.; McIntyre, N. R; and Thompson, M.  “Purification and characterization of enzymes from yeast: an extended undergraduate laboratory sequence for large classes.”  Biochem. Mol. Bio. Ed. 2013, 41, 251-261.

Hougland, J. L.; Hicks, K. A.; Hartmann, H. L.; Kelly, R. A.; Watt, T. J.; and Fierke, C. A.  "Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities."  J. Mol. Bio. 2010, 395, 176-190.

Watt, T. J. and Doyle, D. F.  "ESPSearch: a program for finding exact sequences and patterns in DNA, RNA, or protein."  Biotechniques 2005, 38, 109-115.


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