| Project/Area Number |
63580211
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
生物物性学
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| Research Institution | TOKYO INSTITUTE OF TECHNOLOGY (1989)
The University of Tokyo (1988) |
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Principal Investigator |
IKAI Atsushi FACULTY OF SCIENCE, TOKYO INSTITUTE OF TECHNOLOGY, FULL PROFESSOR, 理学部, 教授 (50011713)
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| Project Period (FY) |
1988 – 1989
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| Project Status |
Completed (Fiscal Year 1989)
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| Budget Amount *help |
¥2,900,000 (Direct Cost: ¥2,900,000)
Fiscal Year 1989: ¥200,000 (Direct Cost: ¥200,000)
Fiscal Year 1988: ¥2,700,000 (Direct Cost: ¥2,700,000)
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| Keywords | BIO-MOLECULAR DEVICE / BIOTECHNOLOGY / HIGHER ORDER STRUCTURE OF PROTEINS / MULTI-FUNCTIONAL PROTEINS / MULTI-FUNCTIONAL ENZYMES / 分子素子 / 生体分子素子 / 集積素子 / 脂肪酸合成酵素 |
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| Research Abstract |
With the aim to establish the designing and constructing principles of integrated molecular system, we studied the structure and working design of biological molecular systems. The model system of our work was animal fatty acid synthetase and alpha-2-macroglobuin, both are multi-functional giant proteins with integrated functional elements. In the case of fatty acid synthetase, seven-enzymes of different partial reactions are integrated into a single functional unit with a definite purpose. When the seven enzymes integrated into two active centers work in a limited space of 20nmxl5nmx7nm, we found that there is a concerted flip-flop type movement of two active centers. Such a movement is probably hydrodynamically coupled with the solvent viscosity and fluctuation as the experimental results on the activity-viscosity relationship clearly indicated. The viscosity dependent movement of the domains and subunits of integrated proteins in large scale will easily be coupled with the chemical rate determining step of the entire reaction. The hydrodynamic coupling between the moving parts of proteins and viscogen molecules added to the aqueous solution of protein was found to be acutely dependent on the size of viscogen. This finding will be exploited in future to estimate the size of the moving elements on the part of the proteins. Similar hydrodynamic coupling of protein movement with solvent is also indicated in the large scale subunit rearrangement of alpha-2- macroglobulin. In this study we made it clear that the hydrodynamic coupling between the elements of integrated system with the solvent is a very important factor to be considered in the design of integrated system on the molecular level.
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