Associate Professor of Chemistry
Department of Chemistry
Faculty, Graduate Program
Studies of protein folding and aggregation
Proteins generally encounter one of two fates after being synthesized. They can fold to their native structure, which enables them to function normally, or they can misfold to a non-native, non-functional structure, which leaves them vulnerable to degradation or aggregation. Protein folding and aggregation are both critically important processes; the former is integral to life, and the latter is strongly associated with devastating diseases, including Alzheimer's and Parkinson's disease. The goal of our research is to improve our understanding of these processes, with an emphasis on energetics and mechanism.
Hurshman, A. R.; White, J. T.; Powers, E. T.; Kelly, J. W. "Transthyretin aggregation under partially denaturing conditions is a downhill polymerization." Biochemistry, 2004, 43, 7365-7381.
Zhang, Q.; Powers, E. T.; Nieva, J.; Huff, M. E.; Dendle, M. A.; Bieschke, J.; Glabe, C. G.; Eschenmoser, A.; Wentworth, Jr. P.; Lerner, R. A.; Kelly, J. W. "Metabolite-initiated protein misfolding may trigger Alzheimer's disease." Proc. Natl. Acad. Sci. USA, 2004, 101, 4752.
Powers, E. T.; Powers, D. L. "A perspective on mechanisms of protein tetramer formation." Biophys J. 2003, 85, 3587-3599.
Colfer, S.; Kelly, J. W.; Powers, E. T. "Factors governing the self-assembly of a beta-hairpin peptide at the air-water interface." Langmuir 2003, 19, 1312-1318.