Association dynamics of transemrbane helices detected by single-molecle FRET
| Project/Area Number |
25460034
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Physical pharmacy
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| Research Institution | Kyoto University |
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Principal Investigator |
Yano Yoshiaki 京都大学, 薬学研究科(研究院), 助教 (60402799)
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| Co-Investigator(Renkei-kenkyūsha) |
KATSUMI Matsuzaki 京都大学, 薬学研究科, 教授 (00201773)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2013: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 膜タンパク質フォールディング / モデル膜貫通へリックス / 一分子FRET / 膜貫通ヘリックス / 一分子計測 / モデル膜貫通ヘリックス / 一分子蛍光エネルギー移動 |
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| Outline of Final Research Achievements |
Membrane proteins are important drug targets. However, driving forces that determine stability of proteins in membranes are poorly understood. In this project, association-dissociation dynamics of transmembrane helices were studied by single molecule FRET in liposomes to elucidate the rule of protein sequences and membrane lipids on helix association. A GXXXG motif was confirmed to drive parallel association of transmembrane helices (AALALAA)3. Moreover, two-transmembrane peptides were found to form four-transmembrane bundle. Membrane cholesterol significantly affected self-association property of the transmembrane helices. These results demonstrate the importance of protein sequence, lipid composition, and their combination on the stability of intramembrane helix-helix interactions.
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Report
(4 results)
Research Products
(8 results)
