| Project/Area Number |
14570103
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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 |
General medical chemistry
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| Research Institution | Hosei University (2004)
Kanazawa University (2002-2003) |
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Principal Investigator |
NAGAI Masako Hosei University, College of Technology, Visiting Professor, 工学部, 客員教授 (60019578)
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| Co-Investigator(Kenkyū-buntansha) |
SAKURAI Hiroshi Kanazawa University, School of Medicine, Professor (2002-,2003), 医学部, 助教授 (00225848)
IMAI Kiyohiro Hosei University, College of Technology, Professor (2004), 工学部, 教授 (50028528)
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| Project Period (FY) |
2002 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2004: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2003: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2002: ¥1,700,000 (Direct Cost: ¥1,700,000)
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| Keywords | hemoglobin / SH3 / near-UV CD / UV resonance Raman / mutants / tyrosine / tryptophan / quaternary structure transition / 高次構造変化 / 芳香族アミノ酸 / 酸素結合機能 / CD / 共鳴ラマン / HbM / アロステリックエフェクター / 蛋白質の機能 / 円二色性(CD) / PI3K / 異常血色素 / SrcSH3 domein / 共鳴ラマン分光 / 円二色性 |
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| Research Abstract |
To get insight into how the quaternary structure changes correlate to their functions, we examined the near-UV CD and UV resonance Raman spectra of hemoglobin and the domein of Src-homology-3 protein with and without ligands. Using four newly synthesized mutant hemoglobins at α42Tyr,α140Tyr,β145Tyr, and/or β37Trp, it was clarified that the main contributors for a negative CD band, a T-sate marker band, are α140Tyr and β145Tyr, located at C-terminal positions. The T-structure specific UV resonance Raman bands of Tyr and Trp were characterized using a natural mutant Hb, Hb M Boston and a Ni-Fe Hybrid hemoglobin.
Src-homology-3(SH3) protein recognize a Pro rich peptides and communicate with the other proteins. We demonstrated that SH3 interacts to the ligand peptide via Tyr residue(s) using UV CD and UV resonance Raman spectoscopy. SH3 has six Tyr residues. Specific Tyr residue for the interaction with Pro-rich peptide was specified as 14Tyr using mutants synthesized in E.coli each Tyr replaced by Ala. Interestingly, Src-SH3 and PI3K-SH3 showed different shtructure changes with the interaction of ligand peptides reflecting the different protein recognition.
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