Figure 2. Free-energy surfaces at T _m as a function of the fractions of intra- and intermolecular contacts formed, computed using various Gō-like models with and without explicit charges and/or 50 mM salt (see Table 2).

Rows A–C, D–F and G–L are for the p53-TAD1/TAZ2, HIF-1α/TAZ1 and NCBD/ACTR complexes, respectively. Q _inter is the fraction of intermolecular contacts formed; Q _p53, Q _HIF-1α and Q _ACTR are the fractions of intramolecular contacts formed by p53-TAD1, HIF-1α and ACTR, respectively; Q _NCBD-tert is the fraction of tertiary intramolecular contacts formed by NCBD (the helical content of NCBD remain similar during coupled binding and folding). Contours are drawn every kT, where k is Boltzmann constant and T is the absolute temperature.