An explanation for the association between proline and amorphous region nanostructural alignment might lie in the capacity for proline to form cross-linkages which disrupt the hydrogen bonds between amorphous region α-helices and other structures causing slippage in the nanostructures under strain . Our finding of a lack of any change in amorphous and lamella region alignment in the silks of protein deprived P. graeffei, despite significant variations in proline composition, across treatments nonetheless suggests that proline does not necessarily directly affect amorphous region nanostructural alignment but likely provides the conditions for the breaking and re-establishment of hydrogen bonds in the region .