ArticleInternational journal of molecular sciences2014
Rise-time of FRET-acceptor fluorescence tracks protein folding.
Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- FRETsael: Nanometer localization of biomolecular interactions using fluorescence lifetime imaging.Biophysical journal · 2025Article
- Intense up-conversion luminescence from DyHeliyon · 2023Article
- Competition between Photoinduced Electron Transfer and Resonance Energy Transfer in an Example of Substituted Cytochrome c-Quantum Dot Systems.The journal of physical chemistry. B · 2021Article
- Spectroscopic Evidence of Energy Transfer in BODIPY-Incorporated Nano-Porphyrinic Metal-Organic Frameworks.Nanomaterials (Basel, Switzerland) · 2020Article
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5 authors.
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Abstract
Uniform labeling of proteins with fluorescent donor and acceptor dyes with an equimolar ratio is paramount for accurate determination of Förster resonance energy transfer (FRET) efficiencies. In practice, however, the labeled protein population contains donor-labeled molecules that have no corresponding acceptor. These FRET-inactive donors contaminate the donor fluorescence signal, which leads to underestimation of FRET efficiencies in conventional fluorescence intensity and lifetime-based FRET experiments. Such contamination is avoided if FRET efficiencies are extracted from the rise time of acceptor fluorescence upon donor excitation. The reciprocal value of the rise time of acceptor fluorescence is equal to the decay rate of the FRET-active donor fluorescence. Here, we have determined rise times of sensitized acceptor fluorescence to study the folding of double-labeled apoflavodoxin molecules and show that this approach tracks the characteristics of apoflavodoxin's complex folding pathway.
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