Nicole Bouley - Graduate Student
B.S. Trinity University, 2007
Our goal is to obtain a fundamental understanding of the critical factors guiding the kinetics and pathways of protein folding. Specifically, we are studying a family of four-helix-bundle cytochrome proteins, including cytochrome c' and cytochrome c-b562. Interestingly, the members of this protein family have similar structures but widely divergent folding pathways. The study of these proteins allows insight in the relationship between amino acid sequence and folding pathways.
My project is to study the folding kinetics of fast-folding cytochrome c-b562 using fluorescent energy transfer (FET), coupled with an ultrafast continuous flow mixer. A highly fluorescent label, dansyl, is covalently attached to various cysteine mutants. The FET rates between the dansyl label and cytochrome heme can provide us with time-dependent distance distributions during the folding process. Thus, an overall picture of the cytochrome c-b562 folding pathway can be obtained.
Faraone-Mennella, J.; Tezcan, F. A.; Gray, H. B.; Winkler, J. R., Stability and folding kinetics of structurally characterized cytochrome c-b562. Biochemistry 2006, 45, (35), 10504-11.