Conformation-dependent energy transfer for chlorophyll-copolypeptide complexes in an aqueous surfactant solution

Spectroscopic and potentiometric studies of chlorophyll a (Chl)-copolypeptide of L-ornithine and L-tyrosine (poly (L-Orn, L-Tyr)) complexes in an aqueous surfactant solution indicate that Chl molecules are incorporated into poly (L-Orn, L-Tyr)-surfactant complexes accompanying a conformational change from a random coil to α-helix and a conformation-dependent energy transfer effectively occurs from the L-tyrosine residue to Chl in the Chl-copolypeptide-surfactant system.