Proximity relations between tyrosine and tryptophan residues in fd phage determined by luminescence measurements.
Resonance energy transfer from tyrosine to tryptophan residues was detected in the phage fd. The magnitude of the transfer efficiency was estimated by both a traditional and an alternative method. The latter involved comparison of the indole acceptor excitation spectrum full-width half-maximum with a set of standard values differing in the amount of absorbance contributed by tyrosine donor. Both methods lead to the same conclusion: essentially all the tyrosine residues of the viral coat are within 0.9 nm of a tryptophan residue. Also, fluorescence lifetime measurements provide additional support for the hypothesis that there are at least two different environments for the coat protein's sole indole side-chain. Little if any DNA phosphorescence was seen, consistent with the nucleic acid bases being stacked in the DNA core.
D003090:Coliphages / Q000032:analysis*; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000032:analysis*; D014443:Tyrosine / Q000032:analysis*; D014764:Viral Proteins / Q000032:analysis*
D014764:Viral Proteins; D014443:Tyrosine; D014364:Tryptophan