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Fluorescence resonance energy transfer at the single-molecule level | Nature Reviews Methods Primers

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Analysing single-molecule fluorescence resonance energy transfer (smFRET) enables an unprecedented view of the dynamics and kinetics of biomolecular conformational changes and interactions. In this Primer, Ha et al. discuss technological advances that have led to smFRET and how the method can be adapted to address various research questions in structural and molecular biology.

Subjects Biophysical methods Single-molecule biophysics Abstract Fluorescence resonance energy transfer (FRET) is a powerful spectroscopic method for measuring distances in the 2–8 nm range. Often, conformational changes and molecular interactions are difficult or impossible to synchronize, or too rare or transient to detect using ensemble FRET. Single-molecule FRET (smFRET) opens new opportunities to probe biomolecular conformational changes or interactions that are missing in static snapshots provided by traditional structural biology tools, as well as to measure the kinetics of these dynami

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