The near ultraviolet circular dichroism of tropomyosin is due to tyrosine and to disulphide bonds. The optical activity of these chromophores can be distinguished by oxidising and reducing the protein. The circular dichroism due to tyrosine is exceptionally intense and is anomalous in that the shape of the spectrum and the wavelength of the maximum are different from those of the absorption spectrum. 2. The intense tyrosyl circular dichroism and the mismatch between circular dichroism and absorption spectra are likely to be due to tyrosine-tyrosine interactions at distances of less than 8 A. 3. The results are analysed in terms of the coiled coil model for tropomyosin and lead to the conclusion that the tyrosines of one helical subunit interact with those of the other. The in-register alignment of the helical chains, with five tyrosines of one chain opposite those of the other, accounts for the tyrosine-tyrosine interactions. 4. The disulphide circular dichroism of oxidized tropomyosin is intense and is consistent with intra-molecular disulphide bonds between helical subunits which can form in the non-staggered model for tropomyosin.
