Abstract
A theory of circular dichroism for the amide transition of polypeptide in random-coil conformation has been developed on the basis of the exciton theory of optical activity and the Monte-Carlo approach to the treatment of statistical systems. This theory has further been extended in such a way as to be applicable for electronic transitions of chromophores bound to the side chains of the random-coil polypeptides. Circular dichroism is calculated for some binding models of acridine orange—random-coil polypeptide complexes. The results are compared with those observed, and it is found that the longer axes of the bound dye molecules are almost parallel or perpendicular to a polypeptide chain, depending on whether ionization of the polypeptide is low or high.
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