| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2018: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2017: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2016: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
|---|
| Outline of Final Research Achievements |
Alpha-synuclein in solution is not folded even under the physiological condition. It becomes the fibril, which causes the Parkinson’s disease. The A30P or A53T mutation is frequently found in the genetically familial patients with the change of the kinetics of the fibril formation.
Amide-proton exchange and signal intensity were employed for the detection of the residual structures. Temperature effects were also obtained for the data. The more flexible structure was observed at the C-terminal region of A30P than WT. By contrast, more rigid structures were observed in mutants at 30-60 region, indicating that the core for the fibril formation was formed. The residual structure even for the intrinsically disordered protein was observed by NMR. The interaction between the N-terminal and C-terminal regions might occur in solution.
|
