| Project/Area Number |
17540383
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics/Chemical physics
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| Research Institution | Osaka University |
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Principal Investigator |
KIKUCHI Macoto Osaka University, Cybermedia Center, Professor, サイバーメディアセンター, 教授 (50195210)
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| Co-Investigator(Kenkyū-buntansha) |
TOKITA Kei Osaka University, Cybermedia Center, Associate Professor, サイバーメディアセンター, 助教授 (00263195)
CHAWANYA Tsuyoshi Osaka University, Graduate School of Information Science and Technology, Associate Professor, 大学院・情報科学研究科, 助教授 (80294148)
TAKAGI Fumiko Osaka University, Cybermedia Center, Invited Researcher, サイバーメディアセンター, 招へい研究員 (60403010)
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| Project Period (FY) |
2005 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2006: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2005: ¥2,400,000 (Direct Cost: ¥2,400,000)
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| Keywords | Ecosystem / Protein / Biophysics / Molecular machine / Computational physics |
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| Research Abstract |
Mainly for ecosystems and proteins, characteristics of the evolutionarily-organized phase-space landscapes are studied using statistical and computational physics.
For ecosystems, general evolutionary dynamics models are analyzed. In special, abundance distributions, e.g. for species in ecosystem, metabolites in cells, proteins and mRNA, is analytically obtained for some parameters of productivity, maturity and abundance of resources. Evolutionary dynamics of HIV virus and human immune system is also studied and the length of the asymptomatic term is obtained for some parameters.
For proteins, we studied free-energy landscape of motor proteins and obtained the following results: (1)We found that large structural fluctuations of kinesin and tubulin are localized at functionally important regions. In particular, our results imply that the microtuble, which is composed of tubulin and plays a role of rail for kinesin, is not just a rail but acts cooperatively in stepping motion of kinesin (papers were submitted). (2) We investigate cooperativity of structural relaxation and nucleotide unbinding of myosin. Our results imply that the binding and unbinding of nucleotide switches the the structures of free-energy landscape (a paper was submitted).
On the above resuls, five papers have been appeard on international journals listed in 11.REFERENCES.
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