Timescales in protein folding accessible with single molecule spectroscopy

Range Figure - link sec
Organism Unspecified
Reference Schuler B, Hofmann H. Single-molecule spectroscopy of protein folding dynamicsexpanding scope and timescales. Curr Opin Struct Biol. 2013 Feb23(1):36-47. doi: 10.1016/j.sbi.2012.10.008. p.37 figure 1PubMed ID23312353
Primary Source See refs beneath figure
Method P.37 caption to figure 1:"Single molecule fluorescence methods, including fluorescence correlation spectroscopy (FCS), cover more than fifteen orders of magnitude in time and allow a wide range of processes relevant for protein folding to be investigated."
Comments P.41 left column 2nd paragraph:"A key benefit of single-molecule experiments is the possibility to extract dynamic information even from equilibrium measurements, which avoids the necessity for a synchronization of the system by perturbation methods, as frequently employed in ensemble experiments. For protein folding, equilibrium dynamics have been obtained, for example, from correlation functions [primary sources 25•, 52, refs 65•, 66 and 71] (Figure 1a), the analysis of broadening and exchange between subpopulations in FRET [Förster resonance energy transfer] efficiency histograms [primary source 30, refs 36•, 37• and 39] (Figure 1b), and from fluorescence trajectories of immobilized molecules [refs 36•, 58••, 66, 67, 68, 72, primary source 73• and ref 74] (Figure 1d). In this way, both the equilibrium distributions and the kinetics can sometimes be obtained from the same measurement." See note beneath figure
Entered by Uri M
ID 112199