All the NH and a-CH proton chemical shifts of alanine oligopeptides (Ac-(Ala),-NHMe, where n = 1 -6 ) with extended and a-helical conformations and anti-parallel / 3 pleated-sheet structure, were calculated by taking into account the magnetic anisotropy effect due to the C=O and two kinds of C-N bond anisotropies, and the electric-field effect. The observed spectral behavior of the NH or CH protons in Ac-Ala-NHMe and Ac-(Ala)2-NHMe could be mostly predicted from the calculation, which indicates that the NH and CH chemical shifts in these oligomers are mainly determined by the intramolecular shielding effect. On the other hand, the appearance of the "doublet a-CH peak" for oligomers with chain lengths of five or more reported by Goodman et al. could not be interpreted in terms of the intramolecular shielding effect. In this case, therefore, whether the CH protons are shielded from the solvent or not, seems to be a dominant factor for the origin of the "doublet peak". The magnetic anisotropy effect of a peptide group was also examined.