An intrinsically disordered protein contains substantial regions that do not adopt one persistent folded structure under the specified conditions. Such regions can bind several partners, acquire structure on binding or support flexible multivalent assemblies. Disorder is therefore compatible with biological function. It is also condition-dependent: a disordered region can change its conformational distribution with binding, modification or environment rather than remaining an entirely structureless chain. [ref]
Phase transitions in the assembly of multivalent signalling proteins by Pilong Li and others. 2012, multivalency and assembly of signalling proteins
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