“…These special geometries are a parallel or antiparallel alignment between sidechain vectors and their orthogonal alignment with respect to backbone HB directions, as was pointed out previously in the study of the self-assembly of dipeptides [ 34 ]. Notably, both conformational states were found as the favorable assembly conformation for the multiple tripeptides was tested and agreed with the crystal structures of several others that had been reported previously [ 16 , 17 , 35 , 36 , 38 ], suggesting that they may be generic conformational features of tripeptides in fibrous assemblies. This finding could have an important implication in the design of assembling tripeptides: these conformations might serve as templates with which the design could begin, especially in a situation in which the design has to otherwise rely on either known experimental structures or a large number of conformational decoys, generated computationally [ 35 ].…”