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Powers, Evan Associate Professor Associate Professor of Chemistry 收藏 完善纠错
The Scripps Research Institute    Department of Chemistry
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研究领域

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.

近期论文

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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.

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