Intrinsically Disordered Protein: Difference between revisions
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[[Image:FoldIndex.jpeg | thumb | FoldIndex<ref name="foldindex">PMID: 15955783</ref> output for three protein sequences (a) Cat-Muscle Pyruvate Kinase (b) The human p53 tumor suppressor protein (c) Chicken gizzard caldesmon; green is folded and red is unfolded]]</td><td>[[Image:DisorderAA.jpg | thumb | Content of order-promoting and disorder-promoting amino acids in the ''Drosophila'' proteome (black) and in the cytoplasmic domain of gliotactin that was shown to be IUP (gray) <ref>PMID: 14579366</ref>]] | [[Image:FoldIndex.jpeg | thumb | FoldIndex<ref name="foldindex">PMID: 15955783</ref> output for three protein sequences (a) Cat-Muscle Pyruvate Kinase (b) The human p53 tumor suppressor protein (c) Chicken gizzard caldesmon; green is folded and red is unfolded]]</td><td>[[Image:DisorderAA.jpg | thumb | Content of order-promoting and disorder-promoting amino acids in the ''Drosophila'' proteome (black) and in the cytoplasmic domain of gliotactin that was shown to be IUP (gray) <ref>PMID: 14579366</ref>]] | ||
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Led by the assumption that “since amino acid sequence determines 3-D structure, amino acid sequence should also determine lack of 3-D structure” <ref name='Dunker2001'>PMID: 11533628</ref> specific sequence features shared by IUPs have been evaluated and algorithms for their identification formulated. | Led by the assumption that “since amino acid sequence determines 3-D structure, amino acid sequence should also determine lack of 3-D structure” <ref name='Dunker2001'>PMID: 11533628</ref> specific sequence features shared by IUPs have been evaluated and algorithms for their identification formulated. | ||