How Robust Is the Mechanism of Folding-Upon-Binding for an Intrinsically Disordered Protein?

ABSTRACT: The mechanism of interaction of an intrinsically disordered protein (IDP) with its physiological partner is characterized by a disorder-to-order transition in which a recognition and a binding step take place. Even if the mechanism is quite complex, IDPs tend to bind their partner in a cooperative manner such that it is generally possible to detect experimentally only the disordered unbound state and the structured complex. The interaction between the disordered C-terminal domain of the measles virus nucleoprotein (N_TAIL) and the X domain (XD) of the viral phosphoprotein allows us to detect and quantify the two distinct steps of the overall reaction. Here, we analyze the robustness of the folding of N_TAIL upon binding to XD by measuring the effect on both the folding

SUBMITTER: Bonetti D 

PROVIDER: S-EPMC5937165 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature