This dataset consists of two types of structures. On one hand, glycine polypeptides in the α-helix and β-strand configurations are considered. On the other hand, polyenoic amino acids and n-amino carboxylic acids are included, which consist of a carboxylic acid and an amine group separated by a conjugated double bond or alkane spacer, respectively. Each of these systems shows characteristic changes of the total dipole moment as the polymer length increases. For the polypeptides, each additional amide bond is itself polar, so that the total dipole increases approximately linearly with the system size. However, the precise behaviour depends on the spatial orientation of these bond dipoles and their interactions, so that the α-helix and β-strand configurations show different scalings. The polyeonic amino acid chains also display a linearly increasing dipole moment. In this case this is not due to the addition of polar bonds, however, but due to the polarization of the delocalized πelectrons in the spacer. Finally, the dipole of the n-amino carboxylic acids remains constant upon increasing the chain length, since no polar bonds or delocalized electrons are present.