Vladimir N. Uversky

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— Intrinsically disordered proteins lack stable tertiary and/or secondary structure under physiological conditions in vitro. They are highly abundant in nature, with ~25-30% of eukaryotic proteins being mostly disordered, and with >50% of eukaryotic proteins and > 70% of signaling proteins having long disordered regions. Functional repertoire of(More)
Intrinsically disordered proteins (IDPs) are associated with a wide range of functions. We suggest that sequence-based subtypes, which we call flavors, may provide the basis for different biological functions. The problem is to find a method that separates IDPs into different flavor / function groups. Here we discuss one approach, the (Charge-Hydropathy)(More)
Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25% amino acid identity at(More)
A data set composed of 1141 proteins representative of all eukaryotic protein sequences in the Swiss-Prot Protein Knowledge base was coded by seven physicochemical properties of amino acid residues. The resulting numerical profiles were submitted to correlation analysis after the application of a linear (simple mean) and a nonlinear (Recurrence(More)
we published our first predictor of intrinsically disordered protein [1]. Since then, we have substantially improved our predictors, and more than 20 other laboratory groups have joined in efforts to improve the prediction of protein disorder. At the algorithmic level, prediction of protein intrinsic disorder is similar to the prediction of secondary(More)
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