2004 Fiscal Year Final Research Report Summary
Relation between the structure and function of proteins studied by the changes of tyrosine and tryptophan residues.
| 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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| Keywords | hemoglobin / SH3 / near-UV CD / UV resonance Raman / mutants / tyrosine / tryptophan / quaternary structure transition |
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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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[Journal Article] Changes in the abnormal α-subunit upon CO-binding to the normal β-subunit of Hb M Boston : resonance Raman, EPR and CD study.2002
Author(s)
Nagatomo, S., Jin, Y., Nagai, M., Hori, H., Kitagawa, T.
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Journal Title
Biophysical Chemistry 98
Pages: 217-232
Description
「研究成果報告書概要(和文)」より
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[Journal Article] Changes in the abnormal α-subunit upon CO-binding to the normal β-subunit of Hb M Boston : resonance Raman, EPR, and CD study.2002
Author(s)
Nagatomo, S., Jin, Y., Nagai, M., Hori, H., Kitagawa, T.
-
Journal Title
Biophysical Chemistry 98
Pages: 217-232
Description
「研究成果報告書概要(欧文)」より
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-
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