Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure.

ABSTRACT: Intrinsically disordered proteins (IDPs) are characterized by a lack of defined structure. Instead, they populate ensembles of rapidly interconverting conformations with marginal structural stabilities. Changes in solution conditions such as temperature and crowding agents consequently affect IDPs more than their folded counterparts. Here we reveal that the residual structure content of IDPs is modulated both by ionic strength and by the type of ions present in solution. We show that these ion-specific structural changes result in binding affinity shifts of up to sixfold, which happen through alteration of both association and dissociation rates. These effects follow the Hofmeister series, but unlike the well-established effects on the stability of folded proteins, they already occur at lo

SUBMITTER: Wicky BIM 

PROVIDER: S-EPMC5604010 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature