Journal of Biophysical Chemistry

Volume 2, Issue 3 (August 2011)

ISSN Print: 2153-036X   ISSN Online: 2153-0378

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Fluorescence quenching of tryptophan and tryptophanyl dipeptides in solution

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DOI: 10.4236/jbpc.2011.23036    6,045 Downloads   11,458 Views   Citations

ABSTRACT

We report measurements of fluorescence quantum yields of tryptophan, tryptophanylaspartate and tryptophanylarginine in several solvents as well as in aqueous solutions over a wide range of pH. We aim to test a computational model developed by Callis and coworkers of fluorescence quantum yield, which postulates that quenching in tryptophan arises from energy loss due to an electron transfer from the aromatic system of tryptophan to one of the amides in the protein backbone. Since the electron transfer state is expected to be high in energy, normally this would not be a possible outcome, but because of its large dipole, such a state should be more accessible in polar solvents. In addition, conditions of low (high) pH, which result in a net positive (negative) charge for the terminal amine (carboxyl) should result in an increase (decrease) of electron transfer rates and low (high) quantum yields. The observed results confirm the predictions of the model.

Cite this paper

Osysko, A. and Muíño, P. (2011) Fluorescence quenching of tryptophan and tryptophanyl dipeptides in solution. Journal of Biophysical Chemistry, 2, 316-321. doi: 10.4236/jbpc.2011.23036.

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