We believe that our approach could be useful in refining fibril structures determined by ssNMR or cryo-EM. This is particularly true for refining disordered or dynamic regions of fibrils, which are difficult to probe using ssNMR and cryo-EM, that could play important roles in initiating aggregation or aberrantly interacting with biological cells. For ssNMR, the final ensemble of structures is visualized by selecting the top 10 or 20 most energetically favorable protein conformers consistent with the experimental constraints applied in the MD simulations. In cryo-EM, disordered, dynamic, or heterogeneous regions could result in poorly resolved electron densities that make it difficult to obtain any structural information at all. In contrast, the widths of dihedral and bond angle distributions measured by Raman spectroscopy naturally give insights into the structural dynamics and conformational heterogeneity of fibrils. This information can be directly incorporated into simulations by parameterizing MD force fields with experimentally measured harmonic force constants, as described above.