Figure 2: Nature of misfolded conformers.
From: Action of the Hsp70 chaperone system observed with single proteins

(a) Fraction of I27 domains attaining unfolded, misfolded and folded conformations upon refolding 8xI27 (n=405) and single I27 (n=25). The refolding data of single I27 domains is the result of experiments performed at different refolding times. The refolding data of 8xI27 have been recorded at steady-state refolding conditions (refolding time 5 s, Supplementary Fig. 2). (b) Cumulative probability distribution of contour lengths of misfolded I27 conformers from steady-state experiments. The binning used was 2 nm. The black line represents control data (n=217), light blue line represents data obtained in the presence of 10 μM DnaJ (n=193), purple line represents data obtained in the presence of 20 μM DnaJ (n=63), red line represents data obtained in the presence of 10 μM DnaK and ATP (n=64), yellow line represents data obtained in the presence of 10 μM DnaK, 10 μM DnaJ and ATP (n=31), green line represents data obtained in the presence of 20 μM lysozyme (n=197). The grey shaded area represents the contour length (28±3 nm, Supplementary Fig. 1c) of one unfolded I27 domain.