Experiment vs. computation: What does nature think of human-designed proteins?

CHED 837

Elizabeth Repasky, beth.repasky@gmail.com1, Brent Dorr2, Carie Fortenberry2, Laura Mizoue2, and Jens Meiler2. (1) Department of Chemistry and Physics, Belmont University, 1900 Belmont Blvd., Nashville, TN 37212, (2) Department of Chemistry, Vanderbilt University, 7330 Stevenson Center, Nashville, TN 37235
A statistical term that accounts for surface-residue solvation of de novo designed proteins has been created in a protein design program, Rosetta. This is done by differentiating between polar surface amino acids and hydrophobic core amino acids. The new alteration in Rosetta Design is tested by creating a de novo four-fold symmetrical TIM barrel design, an alpha-beta barrel fold common in nature. Three rounds of design have led to an improvement of this algorithm through experimental expression and characterization of the designed proteins. A fourth round of design is currently being created to combine the best attributes of each of the previous results.
 

Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster

Division of Chemical Education

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008