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

Figure 1

Modeling disorder in IκBα and thermodynamics.

(A) Crystal structure of the bound-IκBα. (B) Contact-map of bound- and modeled free-IκBα. It can be seen that the repeats 5 and 6 in the modeled free-IκBα (circled region) are dominated by local contacts. (C) The predicted unfolding curve for the free-IκBα with a prominent pre-transition that accounts for ∼20% of the total unfolding amplitude.

Figure 1

doi: https://doi.org/10.1371/journal.pcbi.1003403.g001