Diffusion-limited association of disordered protein by non-native electrostatic interactions.

ABSTRACT: Intrinsically disordered proteins (IDPs) usually fold during binding to target proteins. In contrast to interactions between folded proteins, this additional folding step makes the binding process more complex. Understanding the mechanism of coupled binding and folding of IDPs requires analysis of binding pathways that involve formation of the transient complex (TC). However, experimental characterization of TC is challenging because it only appears for a very brief period during binding. Here, we use single-molecule fluorescence spectroscopy to investigate the mechanism of diffusion-limited association of an IDP. A large enhancement of the association rate is observed due to the stabilization of TC by non-native electrostatic interactions. Moreover, photon-by-photon analysis reveals that

SUBMITTER: Kim JY 

PROVIDER: S-EPMC6226484 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature