ORGN 229 |
| Benjamin F. Cravatt, Departments of Chemistry and Cell Biology, Departments of Chemistry and Cell Biology, Skaggs Institute for Chemical Biology and Scripps Research Institute, La Jolla, CA 92037 |
| The field of proteomics aims to characterize dynamics in protein function on a global scale. However, several classes of enzymes are regulated by posttranslational mechanisms, limiting the utility of conventional proteomics techniques for the characterization of these proteins. Our research group has initiated a program aimed at generating chemical probes that interrogate the state of enzyme active sites in whole proteomes, thereby facilitating the simultaneous activity-based profiling of many enzymes in samples of high complexity. Progress towards the generation and utilization of active site-directed chemical probes for the proteomic characterization of several enzyme classes will be described. These enzyme classes fall into two general categories: 1) enzymes for which active site-directed affinity agents have been well-defined, and 2) enzymes for which active site-directed affinity agents have been lacking. The application of activity-based protein profiling to the functional characterization of enzyme activities that vary in human cancer specimens will be highlighted, as will be the use of this strategy as a screen to discover potent and selective reversible enzyme inhibitors. |
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Alfred Bader Award in Bioinorganic or Bioorganic Chemistry
1:45 PM-5:00 PM, Monday, March 24, 2003 Convention Center -- La Nouvelle Ballroom A/B, Oral
Division of Organic Chemistry |