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However, one should keep in mind that with a very few exceptions, a real protein (not necessary an IDP) has a very sophisticated structural organization characterized by an intricate spatiotemporal heterogeneity, akin to a mosaic or a kaleidoscope, encompassing different functional units with various levels of disorderedness: foldons (independently foldable units), inducible foldons (IDRs that fold upon binding partners), inducible morphing foldons (IDRs that fold differently upon binding to different partners), non-foldons (non-folded regions essential for function), semi-foldons (always partially folded), and unfoldons (ordered regions that must unfold to become active) (Uversky, 2013c;a;b;Jakob et al., 2014)

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TL;DR There is no single answer