De novo design of functional metalloproteins
| Project/Area Number |
25410174
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Bio-related chemistry
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| Research Institution | Nagoya Institute of Technology |
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Principal Investigator |
tanaka tosiki 名古屋工業大学, 工学(系)研究科(研究院), 教授 (70171775)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | デノボタンパク質 / 金属タンパク質 / 銅タンパク質 / 銅配位構造 / EPR測定 / 銅の配位構造 / タイプ３銅タンパク質 / 銅イオン / ブルー銅タンパク質 / デノボ設計タンパク質 / ヘリカルバンドルタンパク質 / 安定性 / ４-へリックスタンパク質 / 酸化還元電位 |
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| Outline of Final Research Achievements |
Natural proteins are usually unstable toward heat and in organic solvents. We introduced couple of disulfide bonds in designed 3-helical bundled proteins. The protein was stable at 90° and in 50% EtOH. As for the design of cupper configuration, we constructed the noble copper configuration using two His and two Cys residues. Hemocyanin has two Cu ions bridged by two oxygens. This site has not constructed in the de novo designed helical proteins. Based on the knowledge obtained in blue copper protein, we utilized a Cys residue for a transient copper binding site, and succeeded to place the two His residues in nearby site. However, bridging by two oxygens was not attained so far. In conclusion, we succeeded in construction of the quite stable scaffold protein structure, noble copper configuration, and two copper proteins in vicinity. Theses techniques are quite promising to construct noble functional proteins, that does not exist in natural proteins, in near future.
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Report
(4 results)
Research Products
(15 results)
