Coupled Binding and Helix Formation Monitored by Synchrotron-Radiation Circular Dichroism.

ABSTRACT: Intrinsically disordered proteins organize interaction networks in the cell in many regulation and signaling processes. These proteins often gain structure upon binding to their target proteins in multistep reactions involving the formation of both secondary and tertiary structure. To understand the interactions of disordered proteins, we need to understand the mechanisms of these coupled folding and binding reactions. We studied helix formation in the binding of the molten globule-like nuclear coactivator binding domain and the disordered interaction domain from activator of thyroid hormone and retinoid receptors. We demonstrate that helix formation in a rapid binding reaction can be followed by stopped-flow synchrotron-radiation circular dichroism (CD) spectroscopy and describe the desig

SUBMITTER: Karlsson E 

PROVIDER: S-EPMC6712486 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature