In this work, the vibrational characteristics of the amide-II modes in beta-peptides in five helical conformations, namely, 8-, 10-, 12-, 14-, and 10/12-helices, have been examined. Remarkable conformational dependence of the amide-II spectral profile is obtained by ab initio computations as well as modeling analysis. Intramolecular hydrogen-bonding interaction and its influence on backbone structure and on the amide-II local-mode transition frequencies and intensities are examined. Through-space and through-bond contributions of the amide-II vibrational couplings are analyzed, and it was found that hydrogen-bonding interaction is not a determining factor for the coupling strength. The results reported here provide useful benchmarks for understanding experimental amide-II infrared spectra of beta-peptides and suggest the potential application of this mode on monitoring the structures and dynamics of beta-peptides.