| Project/Area Number |
21570173
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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
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| Research Institution | Kwansei Gakuin University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
NODA Yasuo 関西学院大学, 理工学部, 教育技術主事 (40268511)
YUTANI Katsuhide 独立行政法人理化学研究所, 理化学研究所播磨研究所, 上級研究員 (90089889)
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| Co-Investigator(Renkei-kenkyūsha) |
SUGIMOTO Hayuki 関西学院大学, 理工学研究科, 博士研究員 (60529527)
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| Project Period (FY) |
2009 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2011: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2010: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2009: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | タンパク質のフォールディング / H/D交換反応とNMR測定 / リゾチームS-S結合欠損変異体 / 超好熱菌由来のタンパク質 / ピロリドンカルボキシルペプチダーゼ / タンパク質の変性状態 / グリセロールによる選択的水和 / タンパク質フォールディング / 超好熱菌由来タンパク質 / H / D交換反応とNMR測定 |
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| Research Abstract |
We have studied partially ordered structures remaining in unstructured disulfide-deficient variants of lysozyme by means of NMR and H/D exchange methods. In this residual structure, two residues of I55 and L56 involved in the bottom of the α-sheet were located in a hydrophobic pocket formed with A, B and C-helices in the β-domain. Lysozyme folding appears to be initiated around this site. On the other hand, H/D exchange reactions were studied in the native state of pyrrolidone carboxyl peptidase(PCP). The native structure was found to be divided into two domains by structural changes near at the residue 70.
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