You can use CD spectroscopy to study the secondary structure and folding properties of your recombinant protein. Furthermore, you can examine protein interactions.
In general, CD give you information about the secondary structure of a protein (helix, sheet, turn/coil). I would assume an experiment studying the CD profile of your protein as a control vs. the same protein recombinant with a drug would tell a great deal about how the drug changes the structure of the protein. More specifically (from my experience) the technique is more sensitive to changes in helicity due to the signature twin dips in the spectra of a helix; meaning the more helical your protein, the more useful CD would be (again, that is a personal opinion from experience)
CD is a nice tool for certain questions. However, I've noticed that quite often people measure CD spectra just for the sake of it when they don't provide any useful information within their study.