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

Förster 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 (λ EX ≈ 280 nm, λ EM ≈ 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…

• NR
  National Research Foundation

  Award: NRF-2012M3A9C4048775
• DU
  Dongguk University
• MO
  Ministry of Science, ICT and Future Planning

  Awards: NRF-2012-0009543, NRF-2012M3A9C4048775
• NR
  National Research Foundation of Korea

  Awards: NRF-2012, 2012M3A9C4048775, NRF-2012M3A9C4048775, NRF-2012-0009543