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Biochemistry. 1991 May 28;30(21):5184-95.

Fluorescence of tryptophan dipeptides: correlations with the rotamer model.

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  • 1Laboratory of Cellular Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.

Abstract

The multiexponential decay of tryptophan derivatives has previously been explained by the presence of rotamers having different fluorescence lifetimes, but it has been difficult to correlate rotamer structure and physical properties. New time-resolved and static data on dipeptides of the type Trp-X and X-Trp, where X is another aminoacyl residue, are consistent with the rotamer model and allow some correlations. That a dominant rotamer of Trp-X zwitterion has the -NH3+ group near the indole ring was inferred from absorption and fluorescence spectra, titrimetric determination of pKa values, photochemical hydrogen-deuterium-exchange experiments, decay-associated spectra, quantum yields, and decay kinetics. Analysis of the lifetime and quantum yield data for Trp dipeptides, especially X-Trp, suggests that static self-quenching is not uncommon. Highly quenched and weak components of the fluorescence do not contribute to the calculated mean lifetime, thus resulting in apparent static quenching. We propose the term quasi-static self-quenching (QSSQ) to distinguish this phenomenon from quenching due to ground-state formation of a dark complex. Mechanisms of quenching and the structure of statically quenched rotamers are discussed. The occurrence of QSSQ supports the idea that rotamers interconvert slowly. A major perceived deficiency of the rotamer model, namely, the apparent inability to predict reasonable rotamer populations from fluorescence decay data, may result from the presence of statically quenched species, which do not contribute to the fluorescence.

PMID:
2036384
[PubMed - indexed for MEDLINE]
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