FLUORESCENCE OF TYROSINE AND TRYPTOPHAN IN PROTEINS USING ONE‐ AND TWO‐PHOTON EXCITATION
- 1 April 1995
- journal article
- Published by Wiley in Photochemistry and Photobiology
- Vol. 61 (4) , 319-324
- https://doi.org/10.1111/j.1751-1097.1995.tb08615.x
Abstract
We examined the emission spectra of tyrosine- and tryptophan-containing proteins using one-photon (270-310 nm) and two-photon (565-610 nm) excitation. Emission spectra for two-photon excitation of native and denatured human serum albumin and of three purine nucleoside phosphorylases indicated an absence of the tyrosine emission normally seen for one-photon excitation below 290 nm. We examined the one-photon and two-photon excitation spectra of tyrosine-tryptophan mixtures to determine the origin of selective excitation of the tryptophan residues. These results confirmed a short-wavelength shift of the tyrosine two-photon excitation spectrum relative to that of tryptophan, as recently reported by Rehms and Callis (1993) Chem. Phys. Lett. 208, 276-282.Keywords
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