ABEL-FRET bridges the timescale gap in single-molecule measurements of the structural dynamics in the A2A adenosine receptor - PubMed
2 days ago
- #ABEL-trapping
- #smFRET
- #GPCR
- ABEL-FRET bridges the timescale gap in single-molecule measurements of structural dynamics in the A2A adenosine receptor.
- Single-molecule Förster Resonance Energy Transfer (smFRET) allows observation of GPCR dynamics at different timescales but is limited to either faster than milliseconds or slower than hundreds of milliseconds.
- Using smFRET with Anti-Brownian Electrokinetic (ABEL) trapping extends observation time of untethered A2A adenosine receptors (A2AAR) in lipid nanodiscs from milliseconds to seconds.
- Conformational heterogeneity in apo and ligand-bound A2AAR was characterized, updating previous estimates of dwell times for long-lived receptor states.
- ABEL-FRET provides valuable insights into GPCR conformational landscapes and dynamics.