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Spectral and polarizational characteristics of rnase c2 unusual fluorescence of tyrosine residues

, : Spectral and polarizational characteristics of rnase c2 unusual fluorescence of tyrosine residues. Molekulyarnaya Biologiya (Moscow) 22(3): 612-623

Unusual spectral and polarizational characteristics have been recorded for RNase C2. The conclusion about tyrosinate participation in the emission of this protein has been made on the basis of comparison of the spectral and X-ray data. It has been shown that the most probable sources of tyrosinate emission are tyrosine residues Tyr-11, -38, -42 and -57. The examination of the ways of decay of the excited states of tyrosine residues of RNase C2 allowed to explain why the contribution of these residues to the emission at the short wavelength part of the spectrum is unessential. The analysis of the X-ray data has confirmed the conclusion that the single tryptophan residue of RNase C2 is located in the non-polar microenvironment. It is shown that the structural fluorescence spectrum of RNase C2 is caused by superposition of the emissions of the tryptophan residue, tyrosine, and tyrosinate.

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