| Project/Area Number |
18310149
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Living organism molecular science
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| Research Institution | Toyama Prefectural University (2007-2009)
The Institute of Physical and Chemical Research (2006) |
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Principal Investigator |
ISOGAI Yasuhiro Toyama Prefectural University, 工学部・生物工学科, 准教授 (00201921)
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| Co-Investigator(Kenkyū-buntansha) |
太田 元規 名古屋大学, 大学院・情報科学研究科, 教授 (40290895)
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| Co-Investigator(Renkei-kenkyūsha) |
OTA Motonori 名古屋大学, 情報文化学部・自然情報学科・複雑システム系, 教授 (40290895)
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| Project Period (FY) |
2006 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥15,820,000 (Direct Cost: ¥13,900,000、Indirect Cost: ¥1,920,000)
Fiscal Year 2009: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2008: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
Fiscal Year 2007: ¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2006: ¥7,500,000 (Direct Cost: ¥7,500,000)
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| Keywords | 蛋白質 / 分子設計 / 立体構造 / フォールディング / 生理活性 / 立体権造 / 機能 |
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| Research Abstract |
The de novo designed Cro protein (Isogai, et al., J.Mol.Biol. 354, 801-814, 2005) and its core variants were synthesized to investigate the sequence dependence of the protein folding. The designed Cro proteins unfold in a non-cooperative, anomalous manner with temperature increased, whereas the native lambda phage Cro protein exhibits cooperative unfolding, in which the secondary structures collapse in the identical time courses. In the designed proteins, α helices gradually disrupted slower than β sheets. The degree of the folding non-cooperativety, or stability of folding intermediate, correlates with the tendency to form insoluble protein aggregate or amyloid fibrils. The present results indicate that amino acid sequences exhibiting cooperative folding can be further selected from the sequences that fold into a well-defined structure, and that the native-like folding properties represent one of the driving forces in naturally occurring sequence selection. Native proteins may have acquired their folding cooperativity under selective pressure to avoid formation of the toxic aggregate or amyloid fibrils in the molecular evolution.
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