The 12-residue tryptophan zipper beta-hairpin (SWTWENGKWTWK) and two C-13-isotopomers were examined in the amide-I region using FTIR and femtosecond two-dimensional infrared (2D IR) spectroscopies. Spectroscopic features of the labeled transitions with C-13-substituted amide unit present in the terminal or turn region of the hairpin, including their frequency shifts and distributions, line broadenings, orientations. and anhartrionicities of diagonal peaks, allow the peptide local structure and local environment to be examined. The results suggest a larger structure fluctuation in the terminal region than in the turn region as a result of the side chain effect and solvent-peptide interaction. The results also suggest that the uncoupled amide-I modes are not degenerate and that this is likely to be a common situation for solvated polypeptides. In addition, the amide-I states in the terminal and turn regions were found to be delocalized over several neighboring amide units. Cross-peaks between the various labeled and unlabeled structural regions were clearly observed in the 2D IR correlation spectra, allowing them to be characterized for monitoring structural changes. These results illustrate the sensitivity of 2D IR to the local environment of solvated peptides. The simulated ID and 2D IR spectra of the hairpin, obtained by using the vibrational exciton model incorporating coupling constants from quantum chemical computations and semiempirical calculations, were found to reproduce the essential features of the experimental results.