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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Alpha-synuclein structures probed by 5-fluorotryptophan fluorescence and 19F NMR spectroscopy.

Alpha-synuclein, the main protein component of fibrillar deposits found in Parkinson's disease, is intrinsically disordered in vitro. Site-specific information on the protein conformation has been obtained by biosynthetic incorporation of an unnatural amino acid, 5-fluorotryptophan (5FW), into the recombinant protein. Using fluorescence and 19F NMR spectroscopy, we have characterized three proteins with 5FW at positions 4, 39, and 94. Steady-state emission spectra (maxima at 353 nm; quantum yields approximately 0.2) indicate that all three indole side chains are exposed to the aqueous medium. Virtually identical single-exponential excited-state decays (tau approximately 3.4 ns) were observed in all three cases. Single 19F NMR resonances were measured for W4, W39, and W94 at -49.0 +/- 0.1 ppm. Our analysis of the spectroscopic data suggests that the protein conformations are very similar in the regions near the three sites.[1]

References

  1. Alpha-synuclein structures probed by 5-fluorotryptophan fluorescence and 19F NMR spectroscopy. Winkler, G.R., Harkins, S.B., Lee, J.C., Gray, H.B. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical. (2006) [Pubmed]
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