| Project/Area Number |
09044319
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| Research Category |
Grant-in-Aid for international Scientific Research
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| Allocation Type | Single-year Grants |
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| Section | Joint Research |
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| Research Field |
General medical chemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
HAMASAKI Naotaka Kyushu University, Faculty of Medicine, Professor, 医学部, 教授 (00091265)
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| Co-Investigator(Kenkyū-buntansha) |
HARASAKI Hiroaki Case Western University, Faculty of Medicine, Professor, 教授
BRUCE Lesley Bristol University, Faculty of Medicine, Associate Researcher, 主任研究員
TANNER Michael Bristol University, Faculty of Medicine, Professor, 教授
IZUHARA Kinji Kyushu University, Faculty of Medicine, Assistant Professor, 医学部, 助手 (00270463)
KANG Donchon Kyushu University, Faculty of Medicine, Associate Professor, 医学部, 助教授 (80214716)
TONNER Micka ブリストル大学, 医学部(英国), 教授
BLOOMBERG Gr ブリストル大学, 医学部, 主任研究員
大久保 研之 九州大学, 医学部, 助手 (40194097)
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| Project Period (FY) |
1997 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥8,100,000 (Direct Cost: ¥8,100,000)
Fiscal Year 1998: ¥3,800,000 (Direct Cost: ¥3,800,000)
Fiscal Year 1997: ¥4,300,000 (Direct Cost: ¥4,300,000)
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| Keywords | Transmembrane / Polytopic membrane Protein / Peptide-lipid interaction / ポリトピック型膜蛋白質 / 疎水性膜貫通領域 / 膜蛋白質構造解析 / ペプチド構造 |
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| Research Abstract |
In this project, we have investigated the band 3 protein structure and function and introduced a novel concept in multi-spanning polytopic membrane proteins revealed by the study on band 3 protein. The transmembrane domain of such proteins can be divided into three categories, that is, hydrophilic loops connecting of transmembrane peptides (category 1), portions being embedded by the peptide-peptide interactions (category 2) and portions being embedded by the peptide-lipid interactions (category 3). Category 2 peptides of polytopic membrane proteins were found to stably reside in the lipid bilayer without peptide-lipid interactions which had been thought to be essential for transmembrane segments. Category 3 peptide is equivalent to the single-spanning segment of a bitopic membrane protein. Three different experiments, that is, a proteolytic digestion method, a chemical modification on band 3 protein and a cell free transcription/translation experiment system, were used to categorize the transmembrane peptides
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