Intrinsically Disordered Protein: Difference between revisions
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The quality of predictions by various algorithms have been evaluated beginning in CASP5 (2002). The assessment of disorder predictions for CASP8 (2008) has been published<ref>PMID: 19774619</ref>. | The quality of predictions by various algorithms have been evaluated beginning in CASP5 (2002). The assessment of disorder predictions for CASP8 (2008) has been published<ref>PMID: 19774619</ref>. | ||
==== Prediction Meta-Servers ==== | |||
Meta-servers gather the predictions from other servers into a single report. | |||
* [http://mobidb.bio.unipd.it/ MobiDB]. The ''Structure'' section in entries at [http://uniprot.org UniProt.Org] offers MobiDB. | |||
* [http://d2p2.pro/ D<sup>2</sup>P<sup>2</sup>]: "pre-computed disorder predictions on a large library of proteins from completely-sequenced genomes. ... statistical comparisons of the various prediction methods ...." | |||
==== Single Algorithm Prediction Servers ==== | |||
* [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.) | ||
