Enzymatic activity from a designed artificial proteome

BIOT 428

Shona C. Patel, scpatel@princeton.edu, Department of Chemical Engineering, Princeton University, Princeton, NJ 08540 and Michael H. Hecht, hecht@princeton.edu, Department of Chemistry, Princeton University, Princeton, NJ 08544.
Enzyme engineering seeks to generate proteins with an enhanced ability for catalysis or binding and often begins with naturally occurring proteins. However, natural proteins have evolved for specific purposes and are already biased towards particular tasks. Proteins that are designed de novo have the potential to be used in a wider variety of bioengineering applications since they have not evolved for specific functions. In order to probe the potential for enzymatic activity within unselected proteins, we are studying a designed artificial proteome comprised of a combinatorial library of de novo, four-helix bundle proteins. By screening proteins that were not designed for any particular function, we determined the likelihood of finding rudimentary activity within the model proteome. Once activity was discovered within the proteome, we implemented directed evolution on selected sequences to improve activity. This approach yielded novel proteins with several types of catalytic activity.
 

Biophysical and Biomolecular Symposium: Protein Engineering
8:00 AM-11:00 AM, Thursday, August 23, 2007 BCEC -- 108, Oral

Division of Biochemical Technology

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007