Recently, we designed and synthesized a new class of profluorescent protease substrates whose spectral properties fit the exciton model; more specifically, spectra of these polypeptides which were doubly labeled with rhodamines showed blue-shifted absorption peaks and fluorescence quenching, both indicators of H-dimer formation. In the work described here NorFES, an undecapeptide which is cleaved by the serine protease elastase, was homodoubly labeled on opposite sides of its cleavage site with six fluorophores in order to identify structural elements of dyes which influence intramolecular H-type dimer formation. Absorption and fluorescence spectra of these six substrates obtained before and after enzymatic cleavage indicate that the exciton band is strongest in the peptide doubly labeled with tetramethylrhodamine, followed by rhodamine-X, and then (diethylamino)coumarin. In contrast, spectra of NorFES homodoubly labeled with fluorescein, hydroxycoumarin, or pyrene do not exhibit exciton bands. These data suggest that factors significant in H-type dimerization are as follows (in decreasing order): delocalized charge, symmetry, and magnitude of the lowest energy electronic transition dipole. Surprisingly, in the group of fluorophores in this study, no evidence for hydrophobic interactions as an important influence was observed.