To ensure an adequate sampling of the model's surface to its surroundings, an extended 2D cuticle surface is needed. This is achieved by replicating the system in both the x and y directions. Similarly to what was done in a single β-sheet, these replicated sheets were crosslinked by means of disulfide bonds using an automated workflow (see section 2.2.2), resulting in additional disulfide bonds. Thus, the resulting protein surface contains both intraand inter-strand disulfide bonds to represent the highly crosslinked protein found in the F-layer of the cuticle . Since our microscopic model incorporates periodicity in all cartesian directions, molecules to be added to the system would interact with the protein slab from above and below. In order to prevent these molecules from potentially interacting with atoms meant to represent the interior of the substrate, we replicated and mirrored the protein slab in the z direction. These slabs were then placed adjacent to each other. Following the same cross linking procedure detailed above, these two protein slabs were then linked together through disulfide bonds. This structure was then used to attach 18-MEA to surface-accessible cysteine residues (Figure ).