Fig. 6
From: Mechanical architecture and folding of E. coli type 1 pilus domains
Folding of oxidized FimHL vs FimHP. a Schematic representation of the polyprotein (I91)2-FimH-(I91)2 construct. b Force-clamp trace of FimH domain. Protein was submitted to a 4-pulse protocol: 60 pN for 5 s + 160 pN for 3 s + 250 pN for 7 s, and 0 pN for 10 s to allow the refolding of the protein. To test if FimH refolded, the first three pulses were applied again. I91 unfolding steps appear as a 25 nm increase in length, meanwhile oxidized FimHL and FimHP yield both a 33 and 32 nm step size increase, respectively, and can be readily differentiated because of the unfolding force pulse regimes. c Refolding probability of FimH at 10 s of quenching time (FimHL, n = 20 and FimHP, n = 17). Bars show the ratio between the trajectories showing refolding and the total number of trajectories. Error bars show the SD of a binomial distribution
