| Project/Area Number |
07409003
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
広領域
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
MORISHIMA Isao Kyoto University, Graduate School of Engineering, Professor, 工学研究科, 教授 (50026093)
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| Co-Investigator(Kenkyū-buntansha) |
TAKAHASHI Satoshi Kyoto University, Graduate School of Engineering, research Associate, 工学研究科, 助手 (30283641)
ISHIMORI Koichiro Kyoto University, Graduate School of Engineering, Associate Professor, 工学研究科, 助教授 (20192487)
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| Project Period (FY) |
1995 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥30,700,000 (Direct Cost: ¥30,700,000)
Fiscal Year 1997: ¥4,800,000 (Direct Cost: ¥4,800,000)
Fiscal Year 1996: ¥5,900,000 (Direct Cost: ¥5,900,000)
Fiscal Year 1995: ¥20,000,000 (Direct Cost: ¥20,000,000)
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| Keywords | Module / Exon Shaffling / Globin / エクソンジャフリング |
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| Research Abstract |
The primary results in this research project are as followa :
(1)Module Substitution in Globins and Peroxidases. The structural and functional properties of the module-substituted globins and peroxidases have been characterized. Most of the module-substituted proteins exhibited highly destabilized protein structure, probably due to the missing or severe perturbation in the key interactions between the modules. The destabilized protein structure also interfered the formation of the specific dimers or tetramers in globins and enzymatic activity in peroxidases. It can be, therefore, concluded that the module-module interactions are also essential to design new stable and functional proteins as well as the module substitution.
(2)Identification of New Module Structure in Globins. The amino acid substituteions based on the structural unit of wchic boundaries are located at the middle of the conventional modules have revealed that the module previously proposed can be divided into new and smaller structural units. In this research project, I focused upon one of the newly identified structural units, which includes the iron-liganded histidine and about 20 amino acid residues in the proximal site, "sub-module m6". The substitution of the sub-module m6 in globins drastically affect the electronic state of heme and configuration of the iron-liganded histidine, indicating that the sub-module m6 would be a "heme binding modules" respondible for the heme binding structure.
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