| Project/Area Number |
20870035
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (Start-up)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
Functional biochemistry
|
|---|
| Research Institution | Kanagawa Institute of Technology |
|---|
Principal Investigator |
KOIKE Ayumi Kanagawa Institute of Technology, 応用バイオ科学部, 准教授 (20454176)
|
|---|
| Project Period (FY) |
2008 – 2009
|
| Project Status |
Completed (Fiscal Year 2009)
|
| Budget Amount *help |
¥3,302,000 (Direct Cost: ¥2,540,000、Indirect Cost: ¥762,000)
Fiscal Year 2009: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2008: ¥1,742,000 (Direct Cost: ¥1,340,000、Indirect Cost: ¥402,000)
|
|---|
| Keywords | 蛋白質 / フォールディング / 酵素 / シャペロン / シャペロニン / GroEL / 反応モデル / 細胞内動態 |
|---|
| Research Abstract |
Chaperonin GroEL is involved in the folding of ～15% of newly translated protein in the cell. To clarify the chaperonin reaction mechanism, we analyzed in detail the symmetric football complexes which is critical intermediate in the reaction cycle, and demonstrated asymmetric diversity of two reaction chambers in the football complexes. We also established key techniques for isolating and detecting the chaperonin complexes formed in the cell, and determined the solution structure of the complexes encapsulating its substrate proteins.
|
