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

CHED 953

Elizabeth Repasky, beth.repasky@gmail.com1, Carie Fortenberry2, Laura Mizoue2, Brent Dorr2, and Jens Meiler3. (1) Department of Chemistry and Physics, Belmont University, 1900 Belmont Blvd., Nashville, TN 37212, (2) Vanderbilt University, (3) Department of Chemistry, Vanderbilt University, 7330 Stevenson Center, Nashville, TN 37235
The protein design program, Rosetta, is multi-faceted. One of the functions of this program is design de novo proteins. It does this through a measurement of the energy functions of proteins; however, it is our goal to augment this energy function to include an environment-dependant statistical term to account for surface-residue solvation during protein folding. Most importantly, this extra statistical term may help in the effort to create a program that will more accurately predict the tertiary structure of proteins. We have chosen to test this alteration by creating a de novo four-fold symmetrical TIM barrel design. This alpha-beta barrel fold is common in nature, it is a relatively simple design, and our de novo design could perhaps provide insight into the evolutionary background of alpha-beta barrel proteins. Expression of our designed protein and testing through x-ray crystallography will allow us to test our program designs and perhaps make improvements.
 

Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, March 26, 2007 Hyatt Regency Chicago -- Riverside Center, Poster

Division of Chemical Education

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