Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.

ABSTRACT: Many intrinsically disordered proteins (IDPs) are significantly unstructured under physiological conditions. A number of these IDPs have been shown to undergo coupled folding and binding reactions whereby they can gain structure upon association with an appropriate partner protein. In general, these systems display weaker binding affinities than do systems with association between completely structured domains, with micromolar K(d) values appearing typical. One such system is the association between α- and β-spectrin, where two partially structured, incomplete domains associate to form a fully structured, three-helix bundle, the spectrin tetramerization domain. Here, we use this model system to demonstrate a method for fitting association and dissociation kinetic traces where, using typica

SUBMITTER: Shammas SL 

PROVIDER: S-EPMC3512043 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature