| Budget Amount *help |
¥94,500,000 (Direct Cost: ¥94,500,000)
Fiscal Year 2011: ¥18,900,000 (Direct Cost: ¥18,900,000)
Fiscal Year 2010: ¥18,900,000 (Direct Cost: ¥18,900,000)
Fiscal Year 2009: ¥18,900,000 (Direct Cost: ¥18,900,000)
Fiscal Year 2008: ¥18,900,000 (Direct Cost: ¥18,900,000)
Fiscal Year 2007: ¥18,900,000 (Direct Cost: ¥18,900,000)
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| Research Abstract |
Protein must fold into unique tertiary structure to achieve its function. However, the folding often competes with intermolecular aggregation, which usually spoils the protein function. Protein aggregates include prions and amyloids, both of which cause fatal neurodegenerative diseases. We investigated following topics; 1) comprehensive aggregation analysis of more than 3,000 Escherichia coli proteins by using a reconstituted chaperone-free translation system, ii) global analysis of chaperone effects, iii) identification of in vivo chaperonin substrates, and iv) in vivo structure and dynamics of yeast prions.
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