| 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 |