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In structural terms, unstructured proteins can be best described as an ensemble of rapidly interconverting alternative conformers. Structural disorder confers advantages onto proteins, such as the increased speed of interaction, the combination of specificity with week and reversible binding, and the ability to carry out more than one function. The molecular functions of IDPs can be classified into six general categories: they either directly stem from disorder (entropic chains), or from transient (display sites, chaperones) or permanent (scavengers, effectors, assemblers) binding of partner molecule(s). Upon binding, IDPs often use short recognition elements in a structurally adaptive process termed disorder-to-order transition or induced folding. Disorder prevails in proteins involved in signal transduction and regulation of transcription, and it also occurs at high levels in proteins involved in diseases. There is conclusive experimental evidence for the disorder of about 500 proteins, collected in the DisProt database, whereas bioinformatics predictions suggest that in eukaryotes the phenomenon of disorder is widespread, with 5-15% of proteins being fully disordered, and about 50% of proteins having at least one long disordered region.

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biochemistry unstructured proteins