Raman spectroscopy of avidin: secondary structure, disulfide conformation, and the environment of tyrosine

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Abstract
An analysis of the amide I region of Raman spectra indicates that [hen egg white] avidin has 10 .+-. 5% and 55 .+-. 4% of its residues in helical and .beta.-strand conformations, respectively. Predictions of secondary structure on the basis of the sequence of avidin are consistent with the high percentage of residues in the .beta. conformation. No differences are observed between the spectra of avidin in solution and in crystals, nor is there a significant difference between the secondary structures of avidin and the complex of avidin with biotin. In addition, the ratio of the intensities of the tyrosine doublet at 826 and 855 cm-1 indicates the lone tyrosine side chain of an avidin subunit is in a strong H-bond as a proton acceptor. The Raman data also indicate that the single disulfide of an avidin subunit has dihedral angles of 0-50.degree. for each of its 2 C.beta..sbd.S bonds and a dihedral angle of 85 .+-. 20.degree. for its S.sbd.S bond. The significance of these results is discussed in relation to findings of earlier work on avidin.