Conformational Studies on C-Phycocyanin from Spirulina platensis

Abstract

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 stepwise unfolding of the protein has been demonstrated. The presence of at least two sets of spectroscopically different chromophores is suggested from the partial denaturation and low temperature experiments. © 1977, Verlag der Zeitschrift für Naturforschung. All rights reserved.