Computer applications in the biosciences · 2005 · 2K citations · 13 references
Life SciencesBiochemistryBioinformaticsComputational BiologyStructural BioinformaticsStructural BiologyIntrinsically Disordered ProteinsProtein Fold RecognitionProtein StructureProtein Structure ModelingComputational Modeling Of Disordered ProteinsDisordered Protein Structure PredictionDisordered ProteinsDisordered Region ModelingIntrinsic Disorder PredictionIntrinsically Disordered Protein ModelingIntrinsically Disordered RegionsProtein Disorder Prediction
Summary: Intrinsically unstructured/disordered proteins and domains (IUPs) lack a well-defined three-dimensional structure under native conditions. The IUPred server presents a novel algorithm for predicting such regions from amino acid sequences by estimating their total pairwise interresidue interaction energy, based on the assumption that IUP sequences do not fold due to their inability to form sufficient stabilizing interresidue interactions. Optional to the prediction are built-in parameter sets optimized for predicting short or long disordered regions and structured domains. Availability: The IUPred server is available for academic users at http://iupred.enzim.hu Contact: zsuzsa@enzim.hu
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Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins
Lilia M. Iakoucheva, Celeste J. Brown, J. David Lawson et al. · Journal of Molecular Biology · 2002 · 1.2K citations
Rune Linding, Lars Juhl Jensen, Francesca Diella et al. · Structure · 2003 · 1.2K citations · Full text