Evolutionary changes in protein structure as models for protein design

CHED 1587

Matthew HJ Cordes, cordes@email.arizona.edu, Department of Biochemistry and Molecular Biophysics, University of Arizona, BSW 436, 1041 E. Lowell St., Tucson, AZ 85721-0088
Proteins are the primary functional molecules in living cells, and the design and reengineering of proteins for novel purposes is of considerable interest. One goal is to design protein switches which change their structural properties in response to stimuli such as changes in solution conditions. One approach is to model such switches on structural changes that occur in the context of natural protein evolution or regulation. We study the Cro family of transcription factors, in which an evolutionary metamorphosis has converted an alpha-helical structure to a mixture of alpha-helix and beta-sheet. P22 Cro and lambda Cro are representatives of the all-alpha and alpha+beta folds, respectively. In the C-terminal 20-25 residues of the domain, two alpha-helices in P22 Cro are replaced by two beta-strands in lambda Cro. We designed ~20 residue "chameleon sequences" which form either alpha-helix or beta-sheet when incorporated as the C-terminus of P22 Cro or lambda Cro, respectively.
 

Exploring and Exploiting Nature with Biomimetics
8:30 AM-11:45 AM, Tuesday, March 27, 2007 McCormick Place North -- Room N230A, Level 2, Oral

Division of Chemical Education

The 233rd ACS National Meeting, Chicago, IL, March 25-29, 2007