Detailed Explanation
Förster Resonance Energy Transfer — a fluorescence technique that measures the distance between two fluorescent labels on a molecule at the 1–10 nanometer scale. When a donor fluorophore is excited and an acceptor is within ~10 nm, energy transfers non-radiatively, causing the acceptor to emit.
FRET efficiency depends on the sixth power of distance, making it an extremely sensitive molecular ruler. In peptide science, FRET is used to study peptide–protein binding, conformational changes, and protease activity (cleavage separates donor from acceptor, changing fluorescence). FRET-based protease assays are widely used in drug screening.
Key Facts
- Förster Resonance Energy Transfer — a fluorescence technique that measures the distance between two fluorescent labels on a molecule at the 1–10 nanometer scale.
- When a donor fluorophore is excited and an acceptor is within ~10 nm, energy transfers non-radiatively, causing the acceptor to emit.
- FRET efficiency depends on the sixth power of distance, making it an extremely sensitive molecular ruler.
- In peptide science, FRET is used to study peptide–protein binding, conformational changes, and protease activity (cleavage separates donor from acceptor, changing fluorescence).
- FRET-based protease assays are widely used in drug screening.
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