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Stephen G. Sligar Professor of Biochemistry, Chemistry, and Biophysics Ph.D. 1975, University of Illinois Structure-Function Relationships in Protein and Nucleic Acid Systems Stephen G. Sligar 116 Morrill, MC-119 405 N. Mathews Urbana, IL 61801 217-244-7395 s-sligar@illinois.edu

The cytochrome P-450 dependent mixed function oxidases play central and crucial roles in mammalian, plant, insect, viral, and microbial metabolism. Central problems being explored relate to the precise bioorganic and bioinorganic chemistry of dioxygen and substrate activation, the identity of metal-oxygen-carbon intermediates, and the structural and functional details of the catalytic event which control recognition and catalysis. Methodologies used include x-ray structure and a variety of biophysical methodologies. Additional NIH funded research focuses on molecular recognition questions, particularly in regard to small molecule, macromolecule and membrane recognition. Major recent efforts focus on the self-assembled Nanodisc system. Central questions relate to the mechanisms of self-assembly, the processes that control integral membrane protein incorporation, control of oliomerization state, fundamental investigations of substrate recognition in the cytochrome P450 monoxygenases, and the mechanisms of G-Protein Coupled Receptor signaling. Human cytochrome P450s involved in drug metabolism and steroid hormone biosynthesis provide another common research theme. We use the Nanodisc technology to aid in isolation, stabilization and functional understanding of drug-drug interactions and regulation and estrogen biosynthesis. A new grant from the Human Frontiers Program focuses on high throughput proteomics of human and plant systems in the use of our Nanodisc system to reveal the entire proteome of protein-protein interactions in complex metabolic pathways of oxidative metabolism.