| Project/Area Number |
62470091
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
高分子物性
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
ANDO Isao Tokyo Institute of Technology Polymer Chemistry Professor, 工学部, 教授 (20016637)
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| Co-Investigator(Kenkyū-buntansha) |
KOMOTO Tadashi Gunma University Biochemical engineering Associate Professor, 工学部, 助教授 (00016643)
NAKAHAMA Seichi Tokyo Institute of Technology Polymer Chemistry Professor, 工学部, 教授 (90016410)
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| Project Period (FY) |
1987 – 1989
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| Project Status |
Completed (Fiscal Year 1989)
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| Budget Amount *help |
¥6,300,000 (Direct Cost: ¥6,300,000)
Fiscal Year 1989: ¥300,000 (Direct Cost: ¥300,000)
Fiscal Year 1988: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1987: ¥5,000,000 (Direct Cost: ¥5,000,000)
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| Keywords | polypeptide / protein / NMR / conformation / liquid crystal / サ-モトロピック液晶 / 金属イオン輸送 / イオノホア / 固体高分解能NMR / NMR化学シフト / コンホメーション / ヘリックス / 水素結合 / 液晶 / サーモトロピック液晶 / 全属イオン輸送 |
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| Research Abstract |
We have demonstrated that solid state ^<13>C and ^<15>N NMR chemical shift values become fundamental data for analyzing conformation of polypeptides in the solid state, solution state and liquid crystalline state. Using the fundamental data, the origin of the formation and no formation of thermotropic liquid crystals for polypeptides with long akyl side chains has been clarified using variable temperature high resolution NMR spectroscopy. Further, higher-order structure of proteins in solution has been determined on the basis of solid state ^<13>C and ^<15>N NMR chemical shift values.
The hydrogen bond plays an important role in forming the stable conformation of polypeptides and proteins. In order to investigate the effect of on the ^<13>C NMR chemical shifts of carbonyl carbons in peptides in the solid state, ^<13>C CP/ MAS NMR spectra were measured for a series of the oligopeptides containing glycine residues of which the crystal structures were already determined by X-ray diffraction We have found that the ^<13>C chemical shifts of the carbonyl carbon in the amide type hydrogen bond form move downfield with a decrease in the hydrogen bond length. This experimental finding is very useful to know the nature of hydrogen bond.
The relationship between the conformation and the biochemical function in biologically-related compounds such as ionophores has been successfully studied by ^<13>C-NMR spectroscopy.
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