Skip to Main Menu Skip to Content

← Return to Personnel Listing

Derek R. Dee

Assistant Professor
  • Food Science & Technology
Mailing Address:
Athens, CAES Campus
Shipping Address:
Athens, CAES Campus

Courses Taught
FDST 4040/6040-4040L/6040 - Food Chemistry
FDST 8070 - Food Proteins and Enzymes

Description of Research Interests

Our research seeks to understand the forces that govern protein structure and function with an emphasis on potential applications in food, biomaterials and medicine. Issues under investigation include enzyme catalysis, protein folding and aggregation, and engineering protein-based nanomaterials. This research involves a variety of biochemical, molecular biology and biophysical approaches and offers a training environment that blends basic and applied sciences to better understand and utilize food proteins and enzymes.

Selected Recent Publications

Dee, D.R., Woodside, M.T. (2016) Comparing the energy landscapes for native folding and aggregation of PrP. Prion, [in press].

Neupane, K., Foster, D.A., Dee, D.R., Yu, H., Wang, F., Woodside, M.T. (2016) Direct observation of transition paths during the folding of proteins and nucleic acids. Science, 352: 239-242.

Yu, H.*, Dee, D.R.*, Liu, X., Brigley, A.N., Sosova, I., Woodside, M.T. (2015) Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape. Proceedings of the National Academy of Sciences of the United States of America, 112: 8308-8313. *co-first authors

Dee, D.R., Myers, B., Yada, R.Y. (2015) Foldase and inhibitor functionalities of the pepsinogen prosegment are encoded within discrete segments of the 44 residue domain. Biochimica et Biophysica Acta – Proteins and Proteomics, 1854: 1300-1306.

Dee, D.R., Horimoto, Y., Yada, R.Y. (2014) Conserved prosegment residues stabilize a late-stage folding transition state of pepsin independently of ground states. PLoS ONE, 9: e101339.

Wang, S.*, Horimoto, Y.*, Dee, D.R., Yada, R.Y. (2014) Understanding the mechanism of prosegment-catalyzed folding by solution NMR spectroscopy. Journal of Biological Chemistry, 289: 697-707. *co-first authors

Yu, H., Dee, D.R., Woodside, M.T. (2013) Single-molecule approaches to prion protein misfolding. Prion, 7: 140-146.

Dee, D.R., Yada, R.Y. (2012) Neutron scattering and the folding and dynamics of the digestive enzyme pepsin. Neutron News, 23: 29-32.

Additional publications can be found here