Skip to main content
. 2019 Jun 20;10:2709. doi: 10.1038/s41467-019-10647-6

Fig. 3.

Fig. 3

The misfolded state has altered kinetics on the ribosome. a Passive data for EF123 shows a short-lived state (N domain) in between the two more distinct states (U, unfolded, at lowest force and M, misfolded, at the highest force). The red dashed line is the HMM fit. b Overlaying the refolding curves from RNC177 (magenta) and EF123 (black) shows they are the same size transition, although EF123 has short-lived N transitions prior to full misfolding. c The folding kinetics of RNC177 are slower and the unfolding kinetics are faster relative to EF123. Diamonds: unfolding rates, circles: folding rates. Error bars are standard error (SE). See Supplementary Table 2 for the fits from the Bell plot shown. RNC177: n = 10 molecules, 111 rate measurements. EF123 (unfolding): n = 14 molecules, 97 rate measurements. EF123 (folding): n = 13 molecules, 88 rate measurements. Source data are provided as a Source Data file