Abstract

A 13C NMR study of some polypeptides containing 13C enriched [2- 13C]glycine (Gly*) residues as a minor component (8%) in the solid state was made in order to clarify a conformational effect on the 13C chemical shifts of the isotropic average value and the principal values of chemical shift tensors (σ 11, σ 22 and σ 33) of glycine methylene carbons (Gly C α) taking antiparallel β-sheet, 3 1-helix, α-helix and ω-helix forms. The latter two conformations are achieved by incorporating Gly residues in the homopolypeptides of other amino acids taking the respective conformations. By selective enrichment with 13C, it was found that the isotropic chemical shifts and principal values of the chemical shift tensor of Gly C α incorporated in some homopolypeptides are displaced depending on their conformations.

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