Fluorescent study of tobacco mosaic virus protein.
Protein fluorescence properties of tobacco mosaic virus [3 Trp residues per monomer (positions 17, 52, 152)] and of two tobacco mosaic virus mutants [green tomato atypical mosaic virus, 2 Trp (52, 152) and cucumber virus4, 1 Trp (unknown position)] have been studied. Emission spectra, fluorescence quantum yields and lifetimes were determined. Results showed that protein fluorescence is due to buried Trp only, except for the cucumber virus4 strain, in which Tyr also contributed to the emission. Comparison of the three strains showed that Trp 17 and Trp 52 have high fluorescence yields (phi17 = 0.29; phi52 = 0.37) whereas Trp 152 (probably present in cucumber virus4) is strongly quenched (phi152 = 0.035). An unusually efficient Tyr leads to Trp energy transfer was observed in tobacco mosaic virus protein, indicating that most of four Tyr residues are located near the highly fluorescent Trp.
D008433:Mathematics; D009029:Mosaic Viruses / Q000032:analysis*; D009154:Mutation; D010942:Plant Viruses / Q000032:analysis*; D011487:Protein Conformation; D013045:Species Specificity; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D014027:Tobacco Mosaic Virus / Q000032:analysis*; D014364:Tryptophan / Q000032:analysis; D014443:Tyrosine / Q000032:analysis; D014764:Viral Proteins
D014764:Viral Proteins; D014443:Tyrosine; D014364:Tryptophan