Mechanisms for polymerization of ovalbumin: X-ray crystallography of initial oligomer
| Project/Area Number |
24580180
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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 |
Food science
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| Research Institution | Kyoto University |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2012: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | タンパク質 / オボアルブミン / アミロイド / コンフォメーション変化 / 認知症 / 熱安定性 / ラセミ化 / D-アミノ酸 / 凝集 / コンフォメーション / コンフォーメーション / 熱重合 / X線繊維回折 |
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| Outline of Final Research Achievements |
Egg ovalbumin has been applied as a model for polymerization or gelation of general food proteins. The mechanisms for polymerization or gelation of the protein have been elucidated by low resolution model with the images like string of beads. Though an atomic resolution model for oligomers of ovalbumin was asked in the present study, good crystal of initial oligomers has not been obtained after a number of trials of purification and preparation under various conditions. On the way of investigation, the authors found the importance of N-terminal segment of the protein on the polymerization process and some solvent-accessible serine residues might be crucial for the thermostability of the protein.
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Report
(4 results)
Research Products
(5 results)
