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Intrinsically disordered proteins (IDPs) are a subset of proteins that lackstable secondary structure. Given their polymeric nature, previous mean-fieldapproximations have been used to describe the statistical structure of IDPs.However, the amino-acid sequence heterogeneity and complex intermolecularinteraction network have significantly impeded the ability to get properapproximations. One such case is the intrinsically disordered tail domain ofNeurofilament low (NFLt), which comprises a 50 residue-long uncharged domainfollowed by a 96 residue-long negatively charged domain. Here, we measure twoNFLt variants to identify the impact of the NFLt two main subdomains on itscomplex interactions and statistical structure. Using synchrotron small-anglex-ray scattering, we find that the uncharged domain of the NFLt inducesattractive interactions that cause it to self-assemble into star-like polymerbrushes. On the other hand, when the uncharged domain is truncated, theremaining charged N-terminal domains remain isolated in solution with typicalpolyelectrolyte characteristics. We further discuss how competing long- andshort-ranged interactions within the polymer brushes dominate their ensemblestructure, and, in turn, their implications on previously observed phenomena inNFL native and diseased states.

From isolated polyelectrolytes to star-like assemblies: The role of  sequence heterogeneity on the statistical structure of the intrinsically  disordered Neurofilament-low tail domain