Accurate structural analysis of natively unfolded proteins by the solution X-ray scattering
| Project/Area Number |
21700322
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
Bioinformatics/Life informatics
|
|---|
| Research Institution | Iwate Medical University (2010)
Nagaoka University of Technology (2009) |
|---|
Principal Investigator |
SEKI Yasutaka Iwate Medical University, 薬学部, 講師 (30377220)
|
|---|
| Project Period (FY) |
2009 – 2010
|
| Project Status |
Completed (Fiscal Year 2010)
|
| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2010: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2009: ¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
|
|---|
| Keywords | 分子シミュレーション / 天然解鎖蛋白質 / 溶液X線散乱法 |
|---|
| Research Abstract |
A new method for generating polypeptide conformations has been developed for studying structural characteristics of unfolded proteins. Those of proteins in high-concentration denaturant solution were analyzed by comparing predictions from this method with results from solution X-ray scattering measurement. Analysis of the dependence of mean square radius on the number of residues and the shape of Kratky profiles for polypeptide chains has confirmed that a high-concentration denaturant solution serves as a good solvent. We found also that, for a conformational ensemble to reproduce experimental data, the probability that main-chain dihedral angles are in the α-region must be in the range of 20 to 40%.
|
Report
(3 results)
Research Products
(9 results)
