The study on peptide and protein syntheses. Infrared spectroscopic conformational analysis of oligo-L-leucines containing only one D-amino acid residue.
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概要
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In order to investigate the influence of a D-amino acid residue on the conformational behavior of peptides and proteins, IR spectroscopic conformational analysis of oligo-L-Leus containing only one D-Ala or D-Val residue was performed in the solid state. For the estimation of their structures, a CPK model and Ramachandran map were very helpful. The D-amino acid residue is clearly inhibited to take the values of the backbone dihedral angles φ and ψ for β-sheet structures formed by L-amino acid residues, while it is allowed for the D-amino acid residue to take the values φ and ψ for helical structures formed by L-amino acid residues. The IR absorption spectroscopic analysis of samples after application of strong shear stress was also useful for the investigation. The effect of shear stress on β-sheet-like structure→helix conformational change is larger for oligo-L-Leus containing a D-Ala residue than those containing a D-Val residue, indicating that the D-Ala residue is more favorable in a helical structure than the D-Val residue. This tendency can be also easily confirmed using CPK model. The significance of this study was discussed in relation to protein synthesis and design of three-dimensional structures of peptides using D-amino acid residues.
- 公益社団法人 日本化学会の論文
著者
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Narita Mitsuaki
Department Of Biotechnology And Life Science Faculty Of Technology Tokyo University Of Agriculture A
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Honda Shinya
Department Of Biological Science And Technology And Tissue Engineering Research Center Tokyo Univers
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Umeyama Hiroshi
Department of Industrial Chemistry, Faculty of Technology, Tokyo University of Agriculture and Technology
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