All-atom conformational sampling of protein-protein interaction
| Project/Area Number |
25840060
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Biophysics
|
|---|
| Research Institution | Yokohama City University |
|---|
Principal Investigator |
MORITSUGU Kei 横浜市立大学, その他の研究科, その他 (80599506)
|
|---|
| Project Period (FY) |
2013-04-01 – 2015-03-31
|
| Project Status |
Completed (Fiscal Year 2014)
|
| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2014: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2013: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
|
|---|
| Keywords | タンパク質相互作用 / 分子動力学シミュレーション / 全原子空間探索 / MSES法 / barnase-barstar複合体 / EIN-HPr複合体 / 常磁性緩和促進 / barnase-barster複合体 |
|---|
| Outline of Final Research Achievements |
Protein-protein interaction is an elementary process of biological phenomena in cell such as signal transduction and transcriptional regulation. In this study, computer simulations of protein complexes were performed, allowing all-atom conformational sampling of the protein-protein interaction processes in solution to be successfully achieved. Statistical-physics-based analyses of the derived structural ensembles yielded a picture of the interaction processes at atomistic level by way of native-interaction formation and desolvation along downhill-like funnel energy landscape. The structural ensemble related to encounter complexes observed from paramagnetic relaxation enhancement experiment was also shown, demonstrating a so-called target-search process leading to the native complex formation via exchanging electrostatic interactions between a pair of protein molecules.
|
Report
(3 results)
Research Products
(7 results)
