Evan Powers, PhD

Institute Investigator
Department of Chemistry


Research Focus

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.


Ph.D. (Organic Chemistry), Massachusetts Institute of Technology, 1999
B.A. (Chemistry), Cornell University, 1992

Professional Experience

2008-2017 Associate Professor of Chemistry, Chemistry, Scripps Research
2000-2008 Assistant Professor, Chemistry, Scripps Research
1999-2000 Research Associate, Chemistry, Scripps Research

Selected References

All Publications

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.