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Intrinsic Tryptophan Fluorescence in the Detection and Analysis of Proteins: A Focus on Förster Resonance Energy Transfer Techniques

Department of Chemistry, Dongguk University, Seoul 100-715, Korea
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Int. J. Mol. Sci. 2014, 15(12), 22518-22538; https://doi.org/10.3390/ijms151222518
Received: 8 October 2014 / Revised: 8 November 2014 / Accepted: 18 November 2014 / Published: 5 December 2014
(This article belongs to the Special Issue Förster Resonance Energy Transfer (FRET) 2015)
F resonance energy transfer (FRET) occurs when the distance between a donor fluorophore and an acceptor is within 10 nm, and its application often necessitates fluorescent labeling of biological targets. However, covalent modification of biomolecules can inadvertently give rise to conformational and/or functional changes. This review describes the application of intrinsic protein fluorescence, predominantly derived from tryptophan (λEX ∼ 280 nm, λEM ∼ 350 nm) , in protein-related research and mainly focuses on label-free FRET techniques. In terms of wavelength and intensity, tryptophan fluorescence is strongly influenced by its (or the proteinlocal environment, which, in addition to fluorescence quenching, has been applied to study protein conformational changes. Intrinsic F resonance energy transfer (iFRET), a recently developed technique, utilizes the intrinsic fluorescence of tryptophan in conjunction with target-specific fluorescent probes as FRET donors and acceptors, respectively, for real time detection of native proteins. View Full-Text
Keywords: FRET; label free detection; tryptophan fluorescence; intrinsic fluorescence; protein imaging; biosensors; immunoassay FRET; label free detection; tryptophan fluorescence; intrinsic fluorescence; protein imaging; biosensors; immunoassay
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Ghisaidoobe, A.B.T.; Chung, S.J. Intrinsic Tryptophan Fluorescence in the Detection and Analysis of Proteins: A Focus on Förster Resonance Energy Transfer Techniques. Int. J. Mol. Sci. 2014, 15, 22518-22538.

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