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Short-range interactions and long-range contacts drive the 3D folding ofstructured proteins. The proteins' structure has a direct impact on theirbiological function. However, nearly 40% of the eukaryotes proteome is composedof intrinsically disordered proteins (IDPs) and protein regions that fluctuatebetween ensembles of numerous conformations. Therefore, to understand theirbiological function, it is critical to depict how the structural ensemblestatistics correlate to the IDPs' amino acid sequence. Here, using small-anglex-ray scattering (SAXS) and time-resolved F\"orster resonance energy transfer(trFRET), we study the intra-molecular structural heterogeneity of theneurofilament low intrinsically disordered tail domain (NFLt). Usingtheoretical results of polymer physics, we find that the Flory scaling exponentof NFLt sub-segments correlates linearly with their net charge, ranging fromstatistics of ideal to self-avoiding chains. Surprisingly, measuring the samesegments in the context of the whole NFLt protein, we find that regardless ofthe peptide sequence, the segments' structural statistics are more expandedthan when measured independently. Our findings show that while polymer physicscan, to some level, relate the IDP's sequence to its ensemble conformations,long-range contacts between distant amino acids play a crucial role indetermining intra-molecular structures. This emphasizes the necessity ofadvanced polymer theories to fully describe IDPs ensembles with the hope itwill allow us to model their biological function.

Intramolecular Structural Heterogeneity altered by Long-range Contacts in an Intrinsically Disordered Protein