Angel C. DeDios is Associate Professor of Chemistry. He teaches General Chemistry I & II, Physical Chemistry I & II, and Nuclear Magnetic Resonance. His research interests are Physical and Biophysical Chemistry. The NMR chemical shift with its intimate relationship with structure and environment (the figure shows the dependence, for example, of the chemical shift of the Ca site in a glycine residue on the torsion angles f and y) is now considered as a powerful tool in the study of molecules of biological importance. Continued success on this front, however, would now require novel experimental data.

Excellent candidates for this much needed data are the peptides (12-30 residues) isolated from the venom of predatory snails belonging to the genus Conus. There are at least 500 species in this group. Each cone snail has in its arsenal a collection of several peptides designed effectively to block a receptor or ion-channel inside its prey, offering an immense diversity of systems (> 5000 peptides) that can be studied. The Conus peptides not only serve as model systems for enhancing present theories of chemical shifts in proteins but are also interesting in their own right. The structure determination of these peptides can be very useful in elucidating structural features of the membrane proteins they bind to. The study of these peptides in the presence of membrane proteins is a long-term goal of this program.