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Intrinsically disordered proteins (IDPs) are functional proteins either fully or partly lacking stable secondary and tertiary structure under physiological conditions that are involved in important biological functions, such as regulation and signalling in eukaryotes, prokaryotes and viruses. The function of many IDPs relies upon interactions with partner proteins, often accompanied by conformational changes and disorder-to-order transitions in the unstructured partner. To investigate how disordered and ordered regions interact when fused to one to another within the same protein, we covalently linked the green fluorescent protein to three different, well characterized IDPs and analyzed the conformational properties of the fusion proteins using various biochemical and biophysical approaches. We observed that the overall structure, compactness and stability of the chimeric proteins all differ from what could have been anticipated from the structural features of their isolated components and that they vary as a function of the fused IDP.