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Submitted on September 5, 2001
Revised on September 11, 2001
Accepted on September 10, 2001

Chemical approaches for functionally probing the proteome

Doron Greenbaum, Amos Baruch, Linda Hayrapetian, Zsuzsanna Darula, Alma Burlingame, Katlin F. Medzihradszky, and Matthew Bogyo

Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94143-0448

Corresponding Author: mbogyo{at}biochem.ucsf.edu

With the availability of complete genome sequences, emphasis has shifted toward the understanding of protein function. We have developed a functional proteomic methodology that makes use of chemically reactive fluorescent probes to profile and identify enzymes in complex mixtures by virtue of their catalytic activity. This methodology allows a comparison of changes in activity of multiple enzymes under a variety of conditions using a single 2D separation. The probes can also be used to localize active enzymes in intact cells using fluorescence microscopy. Furthermore, the probes enable screens for selective small molecule inhibitors of each enzyme family member within crude lysates or intact cells. Ultimately, this technology allows the rapid identification of potential drug targets and small molecule lead compounds targeted to them.


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