Global reconfiguration of protein chain measured by Förster Resonance Energy Transfer (FRET)

Range ≈50 nsec
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. abstract & p.2659 left column 3rd paragraphPubMed ID2417904
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."
Comments Abstract: "Global reconfiguration of the chain occurs on a time scale of approximately equal to 50 ns and slows down concomitant with chain collapse under folding conditions." P.2659 left column 3rd paragraph: "[Investigators'] measurement of the reconfiguration time of ≈50 ns is in good agreement with the relaxation time expected for an ideal chain (refs 59–61) and theoretical estimates of the collapse times for proteins (refs 43, 62)."
Entered by Uri M
ID 112757