| Project/Area Number |
20570118
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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 |
Structural biochemistry
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| Research Institution | National Institute of Advanced Industrial Science and Technology |
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Principal Investigator |
KONDO Hidemasa National Institute of Advanced Industrial Science and Technology, 生物プロセス研究部門, 主任研究員 (80357045)
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| Co-Investigator(Kenkyū-buntansha) |
NISHIMIYA Yoshiyuki 独立行政法人産業技術総合研究所, 生物プロセス研究部門, 主任研究員 (00357716)
TSUDA Sakae 独立行政法人産業技術総合研究所, 生物プロセス研究部門, 研究グループ長 (70211381)
HOSHINO Tamotsu 独立行政法人産業技術総合研究所, 生物プロセス研究部門, 研究グループ長 (60357944)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2010: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2009: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2008: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | X線結晶構造解析 / 不凍タンパク質 / 生物物理 / 微生物 / 極限微生物 / 氷結晶 / 低温生物学 / 環境適応 |
|---|
| Research Abstract |
Antifreeze proteins bind preferentially to the surfaces of embryonic ice crystals and inhibit further growth of ice. In the present study we analyzed three-dimensional structures of microbial antifreeze proteins and revealed their possible ice-binding site by structure-based site-directed mutagenesis. Antifreeze activities measured for various kinds of microbial antifreeze proteins exhibited wide diversity both in thermal hysteresis value and ice crystal shape, in spite of their high sequence homologies. From these observations it is suggested that microbial antifreeze proteins share a common structural scaffold for their interaction with ice and adopt their own antifreeze activities according to their growing environment.
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