Abstract
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are fascinating dynamic conformational ensembles that are observed under physiological conditions. They facilitate a wide variety of biological processes via mechanisms that are distinct from their structured counterparts. Intrinsic disorder enables complex regulation using concerted molecular recognition, posttranslational modification, and alternative splicing. A broad analysis of IDRs reveals their central role in molecular recognition and cellular regulation. The diverse functions of IDRs are complemented by their diverse biophysical properties. Under the single moniker of disorder exist a variety of protein states that vary from protein-to-protein or for the same protein in different biological contexts. The biophysical and functional properties of IDRs are reflected in their composition, sequence complexity, and conservation. These sequence properties have been leveraged to design algorithms that accurately predict intrinsic disorder and certain molecular functions of disorder directly from the protein sequence.
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