Rate constants and mechanisms of intrinsically disordered proteins binding to structured targets.

ABSTRACT: The binding of intrinsically disordered proteins (IDPs) to structured targets is gaining increasing attention. Here we review experimental and computational studies on the binding kinetics of IDPs. Experiments have yielded both the binding rate constants and the binding mechanisms, the latter via mutation and deletion studies and NMR techniques. Most computational studies have aimed at qualitative understanding of the binding rate constants or at mapping the free energy surfaces after the IDPs are engaged with their targets. The experiments and computation show that IDPs generally gain structures after they are engaged with their targets; that is, interactions with the targets facilitate the IDPs' folding. It also seems clear that the initial contact of an IDP with the target is formed by

SUBMITTER: Zhou HX 

PROVIDER: S-EPMC3402904 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature