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 |