To aide in the assignments of low-frequency Raman bands, we performed normal mode analysis on a model amylin 20-29 β-sheet system comprised of two strands. To do this, we initially constructed a 24-mer fibril-like structure of amylin 20-29 using Visual Molecular Dynamics 82 based on structural data obtained using Raman spectroscopy, including backbone ψdihedral and C--O bond angles. The model was then simulated as a parallel β-sheet structure with the ψ-dihedral angle distribution centered at 139 • and the inter-sheet spacing set to 10 Å, as described in detail by Harper et al. The coordinates of the central two peptides in the structure from this model were subsequently used to perform vibrational calculations, as discussed below.