| Project/Area Number |
09558094
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 展開研究 |
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| Research Field |
Biophysics
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| Research Institution | Himeji Institute of Technology |
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Principal Investigator |
NAITO Akira Department of Life Science, Associate Professor, 理学部, 助教授 (80172245)
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| Co-Investigator(Kenkyū-buntansha) |
AIDA Misako Hiroshima University, Faculty of Science, Professor, 理学部, 教授 (90175159)
TUZI Satoru Department of Life Science, Assistant Professor, 理学部, 助手 (60227387)
SAITO Hazime Department of Life Science, Professor, 理学部, 教授 (30100150)
FUJITO Teroaki JEOL Ltd., Department of AI Technology, Section Chief, AI技術部, 課長
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| Project Period (FY) |
1997 – 1999
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| Keywords | Interatomic distance / Dipolar interaction / Three-dimensional structure / REDOR / Molecular dynamics / Membrane bound biomolecule / Isotope labeling / Molecular packing |
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| Research Abstract |
In this research project, we have studied to establish systematic approach in determining the three-dimensional structure of membrane bound biomolecules based on accurate interatomic distances obtained from solid state NMR. Following results were obtained in this research project.
(1) The three-dimensional structure of [ィイD113ィエD1C, ィイD115ィエD1N]-labeled Leu-enkephalin (tyr-Gly-Gly-Phe-Leu) dihydrate crystals was determined on the basis of six sets of accurately determined ィイD113ィエD1C-ィイD115ィエD1N interatomic distances by rotational echo double resonance (REDOR) and some additional constraints from ィイD113ィエD1C chemical shifts.
(2) The phenyl ring dynamics of [ィイD12ィエD1HィイD25ィエD2]PheィイD14ィエD1-labeled LeuィイD15ィエD1- and MetィイD15ィエD1-enkephalin molecules in crystals grown from four solvents were examined using solid state ィイD12ィエD1H NMR spectroscopy. ィイD12ィエD1H NMR powder pattern clearly indicated the presence of 180°flip motions about the Cβ-Cγbond axis of the phenyl rings. The difference of
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the frequencies for the motion was attributed to the manner of their molecular packing in the crystal.
(3) Conformational transition of human calcitonin (hCT) during fibril formation in the acidic and neutral condition were investigated by high resolution solid state ィイD113ィエD1C NMR spectroscopy. The results indicate that conformational transitions from α-helix to β-sheet, and from random coil to β-sheet forms occurred in the central and C-terminus regions, respectively, during fibril formation.
(4) The conformation and dynamics of melittin bound to the dimyristoylphophatidylcholin (DMPC) bilayer and the magnetic orientation in the lipid bilayer systems were investigated by solid-state ィイD131ィエD1P and ィイD113ィエD1C NMR spectroscopy. Using ィイD131ィエD1P NMR, it was found that melittin-DMPC bilayer system forms magnetically oriented elongated vesicles with the long axis parallel to the magnetic field above the liquid crystalline-gel phase transition temperature. ィイD113ィエD1C NMR spectra were observed on the ィイD113ィエD1C labeled melittin bound to the lipid bilayer. Finally, it was found that melittin adopts a transmembrane α-helix whose average axis is parallel to the bilayers normal. Less
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