Alanine oligopeptides provide a key structure of the crystalline domains of the silks from spiders and wild silkworm and also the sequences included in proteins such as antifreeze proteins and amyloids. In this paper, the local dynamics of alanine oligopeptides, (Ala)(3), (Ala)(4), and (Ala)(6) were examined by high-resolution C-13 solid-state NMR. The C-13 spinlattice relaxation times (T(1)s) for the C beta 4 carbons of antiparallel (AP)-beta-sheet (Ala)(4) significantly prolonged and the correlation time was estimated as 3.6 x 10(-1)1 s which was shorter than those of other carbons in the AP-beta-sheet (Ala)(4) (2.8 x 10(10) s). The T-1 values for the C beta carbons of (Ala)(6) showed significantly longer correlation time (8.8 x 10(9) s) than those of AP-beta-sheet (Ala)(4). It is thus revealed that AP-beta-sheet (Ala)(6) exhibited stronger intersheet interaction than those of AP-beta-sheet (Ala)(4). The C-13 spinspin relaxation times (T(2)s) for the C beta 4 carbons showed longer than those of the other C beta 13 carbons of AP-beta-sheet (Ala)4. T2 values of C beta carbons reflect the slow time-scale (similar to 70 kHz) backbone motions. The C-terminal forms strong hydrogen bonds with water molecules and thus the backbone motion is slower than similar to 70 kHz, while the central backbone motions are faster than similar to 70 kHz in the AP-beta-sheet (Ala)(4).