| Project/Area Number |
19540431
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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 |
Biophysics/Chemical physics
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| Research Institution | Kwansei Gakuin University |
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Principal Investigator |
NODA Yasuo Kwansei Gakuin University, 理工学部, 教育技術主事 (40268511)
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| Co-Investigator(Kenkyū-buntansha) |
SEGAWA Shin-ichi 関西学院大学, 理工学部, 教授 (70103132)
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| Project Period (FY) |
2007 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2009: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2008: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2007: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 生物物理 / タンパク質 / リゾチーム / 核磁気共鳴 / ジスルフィド結合 / ランダムコイル / 重水素交換 / ジメチルスルホキシド |
|---|
| Research Abstract |
2SS[6-127, 64-80] variant of lysozyme which has two disulfide bridges and lacks the other two disulfide bridges was quite unstructured in water, but a part of the polypeptide chain was gradually frozen into a native-like conformation with increasing glycerol concentration. It was monitored from the protection factors of amide hydrogens against H/D exchange by means of NMR spectroscopy. With increasing glycerol concentration, some selected regions were further protected. The highly protected residues were included in A-, Band C-helices and β3-strand, and especially centered on Ile 55 and Leu 56. In 2SS[6-127, 64-80], long-range interactions were recovered due to the preferential hydration by glycerol in the hydrophobic box of the α-domain.
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