| Project/Area Number |
02454527
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
結晶学
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| Research Institution | THE INSTITUTE OF PHYSICAL AND CHEMICAL RESEARCH (RIKEN) |
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Principal Investigator |
UEKI Tatuo RIKEN CHIEF SCIENTIST, 生物物理, 主任研究員 (30029954)
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| Co-Investigator(Kenkyū-buntansha) |
FUJISAWA Tetsuro RIKEN SCIENTIST, 生物物理, 研究員 (10231565)
INOKO Yuji OSAKA UNIV. INSTRUCTOR, 基礎工学部, 助手 (00160010)
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| Project Period (FY) |
1990 – 1992
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| Project Status |
Completed (Fiscal Year 1992)
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| Budget Amount *help |
¥6,800,000 (Direct Cost: ¥6,800,000)
Fiscal Year 1992: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1991: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1990: ¥5,400,000 (Direct Cost: ¥5,400,000)
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| Keywords | SOLUTION X-RAY SCATTERING / BIOLOGICAL MACROMOLECULES / ENZYME / STRUCTURE ANALYSIS |
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| Research Abstract |
The structural studies by solution X-ray scattering is to get information as to the overall shape of particle of interest. The recent development of analysis of scattering profile gave much more detailed information if the particle consists of domains or subunits.
The information obtainable is the spatial arrangement of consistent domains or subunits, by the use of scattering profile in rather moderate-angle scattering angles. The present project aims the establishment of experimental system and development of a new analytical procedure. It also consists of biological aspect as to the structural change upon binding of substrate or small molecule.
The detailed structure of DNA coil in the nucleosome core particle isolated from rat thymus. The experiment of contrast variation technique gave scattering only from the DNA molecule, leaving the rest of particle transparent. The structure of DNA molecule is consistent with the result from the low resolution crystal structure analysis. The ras p21 protein, that is related to the development of cancer, was also subjected to the detailed analysis. The structures, with/without GTP molecule, changes slightly, giving different radii of gyration. The surface property also changes appreciably upon GTP binding to the ras p21 protein.
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