Fig. 2: An example time course of reactivation/refolding of soluble rhodanese in a mixture of the chaperones DnaJ/K, GroEL, and GrpE. | Nature Communications

Fig. 2: An example time course of reactivation/refolding of soluble rhodanese in a mixture of the chaperones DnaJ/K, GroEL, and GrpE.

From: How soluble misfolded proteins bypass chaperones at the molecular level

Fig. 2: An example time course of reactivation/refolding of soluble rhodanese in a mixture of the chaperones DnaJ/K, GroEL, and GrpE.The alternative text for this image may have been generated using AI.

Rhodanese was initially unfolded using guanidine hydrochloride and refolding then monitored after a dilution jump and the addition of chaperones. Note that >25% of Rhodanase (red shaded region) is unable to reach its fully folded conformation even in the presence of these chaperones during the time course of the experiment. A kinetic fit (Eq. 1) indicates this subpopulation will take 1016 min (2.35 × 1014 years, 95% Confidence Interval [2.24 × 1014 years, 6.94 × 1014 years] assuming 1% error in the measurements) to fold. Experimental data were extracted from ref. 9 Fig. 4a using PlotDigitizer (see Supplementary Data 1).

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