Intrinsically Disordered Protein: Difference between revisions
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* [http://bioinf.cs.ucl.ac.uk/disopred/ DISOPRED2] (Jones Group, University College London, UK). "DISOPRED2 was trained on a set of around 750 non-redundant sequences with high resolution X-ray structures. Disorder was identified with those residues that appear in the sequence records but with coordinates missing from the electron density map. This is an imperfect means for identifying disordered residues as missing co-ordinates can also arise as an artifact of the crystalization process. False assignment of order can also occur as a result of stabilizing interactions by ligands or other macromolecules in the complex. However, this is the simplest means for defining disorder in the absence of further experimental investigation of the protein." (Quoted from the DISOPRED2 website.) | * [http://bioinf.cs.ucl.ac.uk/disopred/ DISOPRED2] (Jones Group, University College London, UK). "DISOPRED2 was trained on a set of around 750 non-redundant sequences with high resolution X-ray structures. Disorder was identified with those residues that appear in the sequence records but with coordinates missing from the electron density map. This is an imperfect means for identifying disordered residues as missing co-ordinates can also arise as an artifact of the crystalization process. False assignment of order can also occur as a result of stabilizing interactions by ligands or other macromolecules in the complex. However, this is the simplest means for defining disorder in the absence of further experimental investigation of the protein." (Quoted from the DISOPRED2 website.) | ||
* [http://biomine.cs.vcu.edu/servers/flDPnn/ flDPnn] (putative '''f'''unction- and '''l'''inker based '''D'''isorder '''P'''rediction using deep '''n'''eural '''n'''etwork)<ref name="fldpnn">PMID: 34290238</ref>. | * [http://biomine.cs.vcu.edu/servers/flDPnn/ flDPnn] (putative '''f'''unction- and '''l'''inker based '''D'''isorder '''P'''rediction using deep '''n'''eural '''n'''etwork)<ref name="fldpnn">PMID: 34290238</ref>. In 2021, flDPnn, was selected as the best disorder predictor in the first Critical Assessment of Protein Intrinsic Disorder Prediction (CAID) <ref><PMID: 20210419></ref>. | ||
* [https://fold.proteopedia.org/ FoldIndex]<ref name="foldindex" /> (Sussman Group, Weizmann Institute, Rehovot, Israel). FoldIndex makes predictions based on the observation that IDPs occupy the low hydrophobicity/ high net-charge portion of charge-hydrophobicity phase space. (See Figure above.) | * [https://fold.proteopedia.org/ FoldIndex]<ref name="foldindex" /> (Sussman Group, Weizmann Institute, Rehovot, Israel). FoldIndex makes predictions based on the observation that IDPs occupy the low hydrophobicity/ high net-charge portion of charge-hydrophobicity phase space. (See Figure above.) | ||
