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Access to the article is free, however registration and sign-in are required. The availability and abundance of intrinsically disordered proteins inside a cell is under tight control. The cornerstone of modern protein structural biology is the sequence-structure-function paradigm, according to which a protein's function depends on its folding into a unique three-dimensional structure. The discovery of proteins that are wholly disordered or contain lengthy disordered segments, yet are functional (2-6), has wreaked havoc on the lock-and-key world view that demands highly organized proteins. Such disordered proteins are abundant, diverse, vital, dynamic, and chaotic, and on page 1365 of this issue, Gsponer et al. (7) reveal how these disorganized proteins are tightly controlled inside the cell.
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