| Project/Area Number |
26840051
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Biophysics
|
|---|
| Research Institution | Yokohama City University |
|---|
Principal Investigator |
Ito Yuko 横浜市立大学, 生命医科学研究科, 特任助教 (00608698)
|
|---|
| Research Collaborator |
MASAIKE Tomoko 東京理科大学, 理学部応用生物科学科, 講師 (60406882)
|
|---|
| Project Period (FY) |
2014-04-01 – 2017-03-31
|
| Project Status |
Completed (Fiscal Year 2016)
|
| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2015: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
|---|
| Keywords | 分子動力学計算 / F1-ATPase / ATPaseファミリー / 構造変化 / 理論と実験による共同研究 |
|---|
| Outline of Final Research Achievements |
Enzymes of the ATPase family accomplish various functions using ATP hydrolysis energy, which is widely used in all living organisms. All proteins including this important ATPase, proceed their own reaction (function) along with the structural change. So as to understand the ATPase mechanism commonly underlying over ATPase family, the structural change of ATPase were investigated. The structural change of ATPase comprises the three different conformational changes: by ATP binding, by ATP hydrolysis, and by product release. To obtain the whole mechanism, all the steps need to be clarified. The beta subunit of F1-ATPase which has been studied extensively, was selected as representation of the ATPase family protein. Using the MD simulations, all the steps of the conformational change in the beta subunit were revealed. The mechanism obtained here was compared with that of other ATPases.
|
