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