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Updated: Aug 13, 2026

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
Published on: March 14, 2019
Fluorescence energy transfer between nucleotide binding sites in an F-actin filament
Abstract:
Fluorescence energy transfer between nucleotide binding sites in an F-actin filament was measured using 1-N6-ethenoadenosine diphosphate (epsilon-ADP) as a fluorescent donor and 2'(or 3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate (TNP-ADP) as an acceptor, both of which were bound to F-actin. Taking into consideration the helical structure of the F-actin filament, the radial coordinate of the nucleotide binding site was calculated to be 25 A, which corresponds to a distance between these sites along the long-pitch helix of 56.3 A and along the genetic helix of 56.7 A.
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