Tuesday, 6 June 2006 - 10:40 AM Empire C (Hershey Lodge and Convention Center) 388
Rationally designed libraries of novel proteins
Michael H. Hecht, Princeton University, Princeton, NJ
Combinatorial libraries of de novo amino acid sequences can provide a rich source of diversity for the discovery of novel proteins with useful activities. Randomly generated sequences, however, rarely fold into ordered protein-like structures. To enhance the quality of a library, diversity must be focused into regions of ‘sequence space' that favor well-folded structures. We use rational design to produce focused libraries of proteins. Recent experimental work demonstrates that de novo proteins from such libraries – which have neither been selected by evolution, nor designed by computer – fold into native-like structures and display a range of functions. Examples will be presented describing libraries of alpha-helical and beta-sheet proteins. These libraries include well-ordered structures, cofactor binding proteins, catalytically active enzymes, and protein-based biomaterials.