Dr. Scott’s research focus is on the structure and function of human cytochrome P450 enzymes. These membrane enzymes have two types of important physiological roles. Many human P450 enzymes are involved the metabolism of xenobiotics, including procarcinogens and pharmaceutical agents of all kinds. In this context the Scott lab is interested in inhibiting the activation of procarcinogens in vivo (such as those in tobacco smoke) to prevent cancer initiation. Human P450 enzymes are also involved in the synthesis and catabolism of important endogenous compounds such as steroid hormones, fatty acids, retinoic acid, eicosanoids and vitamins. The Scott lab is investigating these P450 enzymes as targets for drug design themselves in specific disease pathways. Recent efforts have particularly focused on understanding the biochemistry and structural biology of CYP17A1, a target for prostate cancer, with efforts toward more effective drug design. Various biochemical, biophysical, and structural biology approaches are used to investigate these versatile enzymes, but with an emphasis on X-ray crystallography and NMR spectroscopy.