Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein

Stan et al. 10.1073/pnas.0700607104.

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SI Figure 6

Fig. 6. (a)Probability distribution [P(H)]of the helix content H of the four-helix bundle in the bulk. The continuous line corresponds to the ensemble of equilibrated conformations at 300 K before folding. The dashed line gives P(H) after the folding reaction is terminated. From this we conclude that the secondary structures are already formed early in the folding process. (b)The solid line shows P(H)for those misfolded conformations that are recognized by GroEL before binding, and the dashed lines correspond to P(H)for the GroEL-bound conformations of the SP. The comparison shows that there is a net loss in the overall helical content when the bulk misfolded conformations bind to the apical domain of GroEL. The simulations were done with l = 1.