Structual formation and structure-function relationship of protein studied with the use peptides
| Project/Area Number |
16550149
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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 |
Chemistry related to living body
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| Research Institution | Kyoto Pharmaceutical University |
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Principal Investigator |
HIROTA Shun Kyoto Pharmaceutical University, Associate Professor, 薬学部, 助教授 (90283457)
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| Project Period (FY) |
2004 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2006: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 2005: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 2004: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | protein / peptide / structure-function relationship / cytochrome c / plastocyanin / tyrosine-containing peptide / electron transfer / 構造形成 / 構造ー機能相関 / シトオクロムc |
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| Research Abstract |
In biosystems, proteins interact with each other. In this research, oligopeptides are used as models of the protein interacting site, and the interaction between the protein and the peptide is studied in detail. The following results are obtained.
1. Cytochrome c(cyt c) was reduced by a tyrosine-containing peptide, tyrosyltyrosylphenylalanine (TyrTyrPhe), at pH 6.0-8.0. Cyt c was reduced at high peptide concentration, whereas the reaction did not occur effectively at low concentration. The reciprocal initial rate constant (1/k_<int>) increased linearly against the reciprocal peptide concentration and against the linear proton concentration, whereas log k_<int> decreased linearly against the root of the ionic strength. These results show that deprotonated (TyrTyrPhe)., presumably deprotonated at a tyrosine site, reduces cyt c by formation of an electrostatic complex.
2. From the MALDI-TOF MS spectra of the reaction products obtained from the reaction between cyt c and YYF, formation of a
… More
quinone and other tyrosine derivatives of the peptide was supported. These products should have been produced from a tyrosyl radical. The results are interpreted that a cyt c_<ox>/(TyrTyrPhe)【tautomer】 cyt c_<red>/(TyrTyrPhe)・ equilibrium is formed, which is usually shifted to the left. This equilibrium may shift to the right by reaction of the produced tyrosyl radical with the tyrosine sites of unreacted TvrTvrPhe peptides.
3. Oxidized plastocyanin (PC) was reduced with TyrTyrTyr at neutral pH. The reciprocal initial rate constant (1/k_<int>) increased linearly with the reciprocal TyrTyrTyr concentration and proton concentration. The results showed that PC was reduced by the deprotonated species of TyrTyrTyr. A linear increase of log k_<int> with increase in the ionic strength was observed due to decrease in the electrostatic repulsion between negatively charged PC and deprotonated (TyrTyrTyr).
These results show that a metalloprotein could be reduced at neutral pH with a tyrosine-containing oligopeptide. Less
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Report
(4 results)
Research Products
(18 results)
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[Journal Article] Conformational changes during apoplastocyanin fokding observed by photocleavable modification and transient grating2006
Author(s)
S.Hirota, Y.Fujimoto, J.Choi, N.Baden, N.Katagiri, M.Akiyama, R.Hulsker, M.Ubbink, T.Okajima, T.Takabe, N.Funasaki, Y.Watanabe, M.Terazima
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Journal Title
J.Am.Chem.Soc. 128・23
Pages: 7551-7558
Related Report
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