The amide I mode is a highly structure sensitive vibration of polypeptides that gives rise to a very strong band in IR absorption and a moderate band in Raman spectra. Many theoretical simulations of IR-band profiles have been undertaken thus far in order to expand the usability of amide I for the structure analysis of peptides and proteins. These simulations have thus far focused on the IR band profiles and to a limited extent on calculating the corresponding vibrational circular dichroism (VCD) signal. In this paper, we use excitonic coupling theory to simulate the IR, isotropic Raman, anisotropic Raman, and VCD band profiles of amide I of parallel and antiparallel beta-sheets as well as of two layers of stacked beta-sheets with antiparallel and parallel orientations of the respective sheets. Our calculations reveal anisotropic Raman and to a lesser extent VCD amide I profiles rather than the corresponding IR profile as suitable tools to discriminate between parallel and antiparallel beta-sheets. Stacking has a very limited influence on the Raman and IR band profiles, but enhance the VCD signal, the sign of which allows one to discriminate between parallel and antiparallel orientations of stacked sheets. Helical twisting and bending of parallel beta-sheets give rise to a very enhanced positive couplet, in agreement with the recent work of Schweitzer-Stenner and Measey (J. Am. Chem. Soc., 2011, 133, 1066). Stochastic uncorrelated inhomogeneity of individual peptide groups causes significant asymmetric broadening of Raman bands and, to a lesser extent, of IR bands and reduces the VCD-couplet of stacked beta-sheets.