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A Disorder-Induced Domino-Like Destabilization Mechanism Governs the Folding and Functional Dynamics of the Repeat Protein IκBα

Figure 4

Domino-like destabilization mechanism in the folding of free-IκBα.

(A) Global unfolding probabilities of helical residues colored according to the repeat identity. (B) The mean residue probabilities (a larger value indicates higher relative stability) as a function of repeat index at 298 and 310 K. The triangles correspond to the control simulation that employs the contact-map of the bound-IκBα, i.e. employing the entire contact-map from the PDB id. 1NFI without deleting interactions. (C) Correlation between the predicted mean residue unfolding probabilities and the fraction of amides exchanged from experiments at 298 K.

Figure 4

doi: https://doi.org/10.1371/journal.pcbi.1003403.g004