2011 Fiscal Year Final Research Report
Protein folding study by real-time folding-unfolding proteolysis
| Project/Area Number |
22710215
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
Living organism molecular science
|
|---|
| Research Institution | Kyoto Prefectural University (2011)
Osaka University (2010) |
|---|
Principal Investigator |
TAKANO Kazufumi 京都府立大学, 大学院・生命環境科学研究科, 教授 (40346185)
|
|---|
| Project Period (FY) |
2010 – 2011
|
| Keywords | 生体高分子 |
|---|
| Research Abstract |
In this work, we examined the slow unfolding pathway of Tk-RNase H2 by pulse proteolysis using a super-stable protease. Through these experiments, we found that Tk-RNase H2 includes two different forms with N-state and N'-state in the native state. The N-state has the large hydrophobic surface in the C-terminal region. In the early stage of unfolding, the N-state changes to an intermediate state(A-state) which is digested by protease at the C-terminal region. In contrast, the N'-state is a protease resistant form. In the slow unfolding pathway, the A-state shifts to the N'-state which gradually unfolds.
|
