The chromophore-protein interactions of C-phycocyanin (C-PC) from Spirulina platensis have been studied by following the partial and complete denaturation with UV-Vis spectroscopy. From comparison with published MO calculations, an elongated conformation of the chromophore is suggested for native C-PC, a cyclic one for denatured C-PC. By means of partial denaturation, a step wise unfolding of the protein has been demonstrated. The presence of at least two sets of spectro scopically different diromophores is suggested from the partial denaturation and low temperature experiments.
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Scheer et al. (1977) studied this question.