Our research involves the protein-folding problem. Simply stated, we wish to predict the three-dimensional structure of a protein from a consideration of amino acid sequence. This involves mathematical models, high-speed computers, computer graphics, and more recently the tools of artificial intelligence computer languages. We are currently working in two directions: Improving algorithms for the prediction of secondary structure (alpha- helices and beta-strands), and applying existing techniques to predict the three-dimensional structure of cytokines and other largely helical proteins. Proteases from a variety of parasites are being studied as targets for rational drug design. Particular emphasis has been placed on the development of antimalarial therapies. |
Li, Z., Chen, X., Davidson, E., Zwang, O., Mendis, C., Ring, C.S., Roush, W.R., Fegley, G., Li, R., Rosenthal, P.J., Lee, G.K., Kenyon, G.L., Kuntz, I.D., Cohen, F.E. (1994). Anti-malarial drug development using models of enzyme structure. Chemistry and Biology 1: 31-37.
Lichtarge, O., Bourne, H.R. and Cohen, F.E. (1996). Evolutionary trace method defines binding surfaces common to protein families. J. Molec. Biol. 257: 342-358.
Lichtarge, O., Bourne, H.R. and Cohen, F.E. (1996). Evolutionarily conserved Gabg binding surfaces support a model of the G protein-receptor complex. Proc. Natl. Acad. Sci., U.S.A. 93: 7507-7511.
information last updated February 2003 |
Biomedical Sciences (BMS) Graduate Program
