| Project/Area Number |
13480214
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Biophysics
|
|---|
| Research Institution | Keio University (2002)
The University of Tokyo (2001) |
|---|
Principal Investigator |
NAKASAKO Masayoshi Faculty of Science and Technology, Department of Physics, Associate Professor, 理工学部, 助教授 (30227764)
|
|---|
| Project Period (FY) |
2001 – 2002
|
| Project Status |
Completed (Fiscal Year 2002)
|
| Budget Amount *help |
¥8,800,000 (Direct Cost: ¥8,800,000)
Fiscal Year 2002: ¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 2001: ¥6,700,000 (Direct Cost: ¥6,700,000)
|
|---|
| Keywords | Proteins / protein hydrations / Cryogenic Crystallography / Molecular dynamics simulation / qlass transition / bio-informatics / バイオイオンフォマティクス / バイオインフォマティクス / 蛋白質 / 水和構造 / 低温結晶解析 / 蛋白質水和 / X線結晶構造解析 |
|---|
| Research Abstract |
Hydration of protein is one of the most important subjects to study the function, folding and dynamics of the protein. Among many techniques investigating hydration structures of proteins, cryogenic X-ray crystallography and molecular dynamics simulation have provided much information on protein hydration. In this project, I studied the static and dynamical characteristics of hydration structures of proteins. In particular, in the crystal structure analysis of glutamate dehydrogenase, I observed the dynamical coupling of hydration structural changes and the domain motion. This is the first experimental evidence to reveals such coupling in protein motion. In addition I investigated the glassy transition occurring around 160 K for human lysozyme. Through molecular dynamics simulations of proteins, we found the selective orientation of water dipoles on the surface of proteins. The results of the present research may provide new insights into the dynamics and folding of proteins in aqueous solution.
|
