Time for transition between protein activation/inactivation states

Range 100-200 µsec
Organism Bacteria Thermotoga maritima
Reference Chung HS, Louis JM, Eaton WA. Feature Article: Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories. Proc Natl Acad Sci U S A. 2009 Jul 10PubMed ID19584244
Primary Source Rhoades E, Cohen M, Schuler B, Haran G. Two-state folding observed in individual protein molecules. J Am Chem Soc. 2004 Nov 17 126(45):14686-7.PubMed ID15535670
Method (of primary source:) The cold-shock protein from Thermotoga maritima (CspTm) was labeled with a green-fluorescing and a red-fluorescing dye, serving as FRET donor and acceptor, respectively. FRET upon excitation by a laser beam allows folded and unfolded molecules to be distinguished on the basis of the strong distance dependence of energy transfer between the chromophores.
Comments Researchers' results provide an upper bound of ~200 µs for this transit time, which is in agreement with the simple assumptions made in previous analyses of protein folding.
Entered by Uri M
ID 104596