Time scale of fluorophore reorientation in Förster Resonance Energy Transfer (FRET)

Range ≈300 psec
Organism Generic
Reference Nettels D, Gopich IV, Hoffmann A, Schuler B. Ultrafast dynamics of protein collapse from single-molecule photon statistics. Proc Natl Acad Sci U S A. 2007 Feb 20 104(8):2655-60. p.2656 right column 2nd paragraphPubMed ID2417904
Primary Source [19] Schuler B, Lipman EA, Steinbach PJ, Kumke M, Eaton WA. Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence. Proc Natl Acad Sci U S A. 2005 Feb 22 102(8):2754-9.PubMed ID15699337
Method Abstract: "[Investigators] use the statistics of photon emission from single molecules to probe the ultrafast dynamics of an unfolded protein via Förster resonance energy transfer." Primary source abstract: "To determine whether Forster resonance energy transfer (FRET) measurements can provide quantitative distance information in single-molecule fluorescence experiments on polypeptides, [investigators] measured FRET efficiency distributions for donor and acceptor dyes attached to the ends of freely diffusing polyproline molecules of various lengths."
Comments P.2656 right column 2nd paragraph: "Fluorophore reorientation occurs on the time scale of ≈300 ps (primary source) resulting fluctuations in the energy transfer rate would thus affect the correlation functions only on time scales much shorter than the range relevant for the dynamics investigated here."
Entered by Uri M
ID 112756