Abstract
The fluorescence lifetime and rotational correlation time of the single tryptophan residue in α-cobratoxin have been measured between pH 2 and 10. The fluorescence decays are non-exponential and give lifetimes that are shorter than normally observed in small proteins (0.3 ns and 1 ns). This emission is consistent with a model in which the tryptophan residue is in slightly different environments in the protein. Fluorescence anisotropy decays show that the tryptophan residue is almost completely immobilised by neighbouring groups in the protein. The range of the “wobbling” motion is slightly pH dependent and limited to between 5° and 10°.
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Beddard, G.S., Tran, C.D. Fluorescence studies of the restricted motion of tryptophan in α-cobratoxin. Eur Biophys J 11, 243–248 (1985). https://doi.org/10.1007/BF00262001
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DOI: https://doi.org/10.1007/BF00262001