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