Nature Communications (Oct 2022)

Binary-FRET reveals transient excited-state structure associated with activity-dependent CaMKII - NR2B binding and adaptation

  • Tuan A. Nguyen,
  • Henry L. Puhl,
  • Kirk Hines,
  • Daniel J. Liput,
  • Steven S. Vogel

DOI
https://doi.org/10.1038/s41467-022-33795-8
Journal volume & issue
Vol. 13, no. 1
pp. 1 – 14

Abstract

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FRET can be used to study conformational changes and protein-protein interactions. Here the authors report Binary-FRET for monitoring two FRET reactions, one encoded in the fluorescence lifetime of the donor, another encoded in its anisotropy, and monitor the dynamics of CaMKII and its interaction with NR2B.