We report the results of the first investigation on the effect of polarity on the elastic properties of an elastomeric protein resilin found in different insects. We simulate tensile tests on four naturally occurring resilin motifs. We repeat simulations on reduced-polarity counterparts of these motifs by setting the charge on each atom to zero, setting the charge on each atom to one-half of the natural value, as well as by replacing all of the polar amino acids with non-polar substitutes. The results highlight a strong correlation between polarity and extensibility. This is due to the presence of adsorbed water molecules that assist deformation energy transfer from the polar motif, allowing it to stretch further before it undergoes failure. These results unambiguously characterize the influence of charge on the mechanical properties of proteins, thus creating pathways for future formulations of novel bioinspired elastomeric rubbers.