A NMR Study of Individual Residues of Proteins in a Random Coil State
| 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 |
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| 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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Report
(4 results)
Research Products
(33 results)
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[Journal Article] Glycerol-Induced Folding of Unstructured Disulfide-Deficient Lysozyme into a Native-Like Conformation2009
Author(s)
Sakamoto, K., Hirai, K., Kitamura, Y., Yamazaki, K., Yusa, M., Tokunaga, N., Doi, G., Noda, Y., Tachibana, H., Segawa, S
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Journal Title
Biopolymers 91
Pages: 665-675
Related Report
Peer Reviewed
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[Journal Article] The Confirmation of the Denatured Structure of Pyrrolidone Carboxyl Peptidase under Nondenaturing Conditions: Difference in Helix Propensity of Two Synthetic Peptides with Single Amino Acid Substitution2008
Author(s)
Umezaki, T., Iimura, S., Noda, Y., Segawa, S., Yutani, K
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Journal Title
Proteins: Structure, Function, and Bioinformatics 71
Pages: 737-742
Related Report
Peer Reviewed
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[Journal Article] Characterization of the Denatured Structure of Pyrrolidone Carboxyl Peptidase from a Hyperthermophile under Nondenaturing Conditions: Role of the C-Terminalα-Helix of the Protein in Folding and Stability2007
Author(s)
Iimura, S., Umezaki, T., Takeuchi, M., Mizuguchi, M., Yagi, H., Ogasahara, K., Akutsu, H., Noda, Y., Segawa, S., Yutani, K
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Journal Title
Biochemistry 46
Pages: 3664-3672
Related Report
Peer Reviewed
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