| Project/Area Number |
05303002
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| Research Category |
Grant-in-Aid for Co-operative Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
Physical chemistry
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| Research Institution | Himeji Institute of Technology |
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Principal Investigator |
SAITO Hazime Himeji Inst.of Tech., Dept.of Life Sci., Profess, 理学部, 教授 (30100150)
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| Co-Investigator(Kenkyū-buntansha) |
ASAKURA Tetsuo Tokyo U.of Agr.& Tech.Dept.of Biotech.Profess, 工学部, 教授 (30139208)
HIKICHI Kunio Hokkaido University Dept.of Biol.Sci., Profess, 理学部, 教授 (30000805)
ANDO Isao Tokyo Inst.of Tech., Dept.of Polym.Chem., Profess, 工学部, 教授 (20016637)
NOZAWA Tsunenori Tohoku University, Dept.of Chem., Profess, 工学部, 教授 (10006322)
TERAO Takehiko Kyoto University, Dept.of Chem., Profess, 理学部, 教授 (50093274)
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| Project Period (FY) |
1993 – 1994
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| Keywords | High-resolution Solid-state NMR / Structural Biology / Distance information / 3D Structure / Biomolecules |
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| Research Abstract |
Three dimensional structures of biomolecules have been explored either by the non-empirical or empirical means.
Non-empirical determinations for 3D structures of biomolecules Interatomic distances of cchemically synthesized[^<13>C,^<15>N]-doubly labeled peptides which are four-or seven-bonds apart were determined with accuracy of 0.02A by means of Rotational Echo Double Resonance(REDOR). Subsequently, three dimensional structure of a tripeptides was revealed based on the data of the interatomic distance alone(Saito). It was pointed out the interatomic distances were determined with accuracy of 0.002A by careful analysis of Pake doublet, as far as the direct chemical bond is concerned(Terao). Fujiwara explored a new means to determine the torsion angles of the peptide bonds by means of magnetization transfer via J couplings. Further, Asakura showed that 3D structure of highly oriented biomolecules such as silk fibroin is revealed by careful analysis of angular dependency of chemical shift tensor.
Empirical determination for 3D structure of biomolecules Ando showed that empirical correlations of chemical shifts with hydrogen-bond distances are very useful for an empirical determination of 3D structure of biomolecules. Further, Shoji examined a correlation between ^<13>N chemical shifts and their secondry structures. Complex crystals of bacterial celluloses were carefully examined by ^<13>C NMR.A study on interaction between chromophore and proteins has been done with emphasis on study of photosynthesis.Interaction between collagen and inorganic mineral for hard tissue was also examined by ^<13>C NMR spectroscopy(Hikichi).
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