The xcexb2 roll molecules with sequence (GAGAGAGQ)10 stack via hydrogen bonding to form fibrils which have been themselves been used to make viral capsids of DNA strands, supramolecular nanotapes and pH-responsive gels. Accelerated molecular dynamics (aMD) simulations are used to investigate the unfolding of a stack of two xcexb2 roll molecules, (GAGAGAGQ)10, to shed light on the folding mechanism by which silk-inspired polypeptides form fibrils and to identify the dominant forces that keep the silk-inspired polypeptide in a xcexb2 roll configuration. Our study shows that a molecule in a stack of two xcexb2 roll molecules unfolds in a step-wise fashion mainly from the C terminal. The bottom template is found to play an important role in stabilizing the xcexb2 roll structure of the molecule on top by strengthening the hydrogen bonds in the layer that it contacts. Vertical hydrogen bonds within the xcexb2 roll structure are considerably weaker than lateral hydrogen bonds, signifying the importance of lateral hydrogen bonds in stabilizing the xcexb2 roll structure. Finally, an intermediate structure was found containing a xcexb2 hairpin and an anti-parallel xcexb2 sheet consisting of strands from the top and bottom molecules, revealing the self-healing ability of the xcexb2 roll stack.