Figure 6: Schematic illustration of the templated folding mechanism.
From: Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein
The analysis of the thermodynamic and structural features of the folding upon binding mechanism of c-Myb reveals that this IDP folds via a templated mechanisms, which involves a heterogeneous nucleation process induced by the structural features of the ligand. This view implies a structural malleability of the transition state, which contrasts the robustness typically observed in the folding pathway of globular proteins, where the transition state forms by a spontaneous nucleation process (homogeneous nucleation) and is a distorted version of the native state with a highly conserved fraction of native-like contacts19,21,23.
