<P> An intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three - dimensional structure . IDPs cover a spectrum of states from fully unstructured to partially structured and include random coils, (pre -) molten globules, and large multi-domain proteins connected by flexible linkers . They constitute one of the main types of protein (alongside globular, fibrous and membrane proteins). </P> <P> The discovery of IDPs has challenged the traditional protein structure paradigm, that protein function depends on a fixed three - dimensional structure . This dogma has been challenged over the 2000s and 2010s by increasing evidence from various branches of structural biology, suggesting that protein dynamics may be highly relevant for such systems . Despite their lack of stable structure, IDPs are a very large and functionally important class of proteins . In some cases, IDPs can adopt a fixed three - dimensional structure after binding to other macromolecules . Overall, IDPs are different from structured proteins in many ways and tend to have distinct properties in terms of function, structure, sequence, interactions, evolution and regulation . </P>

Intrinsically disordered regions typically lack hydrophobic amino acids