beta-Strand peptides are known to assemble into either antiparallel (AP) or parallel (P) beta-sheet forms which are very important motifs for protein folding and fibril formations occurring in silk fibroin or amyloid proteins. Well-resolved H-1 NMR signals including NH protons were observed for alanine tripeptides (Ala)(3) with the AP and P structures as well as (Ala)(n) (n = 4-6) by high-field/fast magic-angle spinning NMR. Amide NH and amino NH3+ H-1 signals of (Ala)(3) with the P structure were well resonated at 7.5 and 8.9 ppm, respectively, whereas they were not resolved for the AP structure. Notably, NH H-1 signals of (Ala)(3) and (Ala)(4) taking the P structure are resonated at higher field than those of the AP structure by 1.0 and 1.1 ppm, respectively. Further, NH N-15 signals of (Ala)(3) with the AP structure were resonated at lower field by 2 to 5 ppm than those of (Ala)(3) with the P structure. These relative H-1 and N-15 hydrogen bond shifts of the P structure with respect to those of the AP structure are consistent with the relative hydrogen bond lengths of the interstrand N-H center dot center dot center dot OC bonds. Distinction between the two crystallographically independent chains present in the AP and P structures was feasible by N-15 chemical shifts but not by H-1 chemical shifts because of insufficient spectral resolution in the latter. Calculated H-1 and N-15 shielding constants by density functional theory are generally consistent with the experimental data, although some discrepancies remain depending upon the models used.