Structural analysis of protein using synchrotron-radiation vacuum-ultraviolet circular dichroism and study of biomolecular interactions(Fostering Joint International Research)
| Project/Area Number |
15KK0260
|
|---|
| Research Category |
Fund for the Promotion of Joint International Research (Fostering Joint International Research)
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Biophysics
|
|---|
| Research Institution | Hiroshima University |
|---|
Principal Investigator |
Matsuo Koichi 広島大学, 放射光科学研究センター, 准教授 (40403620)
|
|---|
| Research Collaborator |
Woody Robert W. コロラド州立大学, 生化学・分子生物専攻, 名誉教授
|
|---|
| Project Period (FY) |
2016 – 2017
|
| Project Status |
Completed (Fiscal Year 2017)
|
| Budget Amount *help |
¥8,320,000 (Direct Cost: ¥6,400,000、Indirect Cost: ¥1,920,000)
|
|---|
| Keywords | 放射光円二色性 / アミロイド線維 / 分子動力学法 / CD理論 / 蛋白質‐蛋白質相互作用 / 分子間構造 / 円二色性 / 蛋白質 / 分子動力学 / 放射光 / 溶液構造 / 真空紫外領域 / アミノ酸側鎖構造 / 高次構造 / 生物物理 / 量子ビーム / 神経科学 / バイオ関連機器 |
|---|
| Outline of Final Research Achievements |
Circular dichroism (CD) theory can calculate the CD spectrum of protein from its three-dimensional structure at atomic level. In this study, we improved this theory as the structural information of amino-acid side chain (tertiary structure) and backbone (secondary structure) can be more accurately characterized. New theory was evaluated by the crystal structures of seventeen proteins by comparing their experimental and theoretical spectra. This method was applied to the structural analysis of amyloid fibrils of beta2-microglobulin fragment at two pH values (acid and base conditions). The results showed that the structural differences depending on pH were ascribed not to the secondary structures but to the intermolecular structures related to side chain of amino acids, indicating that the CD theory including the VUV region was powerful tool for the structural research of protein-protein interactions such as amyloid fibrils.
|
Report
(3 results)
Research Products
(24 results)
