title: The contribution of intrinsic disorder prediction to the elucidation of protein function.
abstract: Current knowledge of protein function stems primarily from the detailed characterization of some protein domain families and from extensive homology-based annotation transfers. Intrinsically disordered proteins exploit complementary molecular recognition mechanisms and their study has potential to make a significant contribution to the field. Building on established computational biology techniques, efforts are now aimed at unveiling their biological roles at the molecular and system level. Recent developments towards identifying functional sites in disordered regions, and analysing how the occurrence of protein disorder in a gene can provide insight into its biochemical and cellular function are discussed.
authors: Bioinformatics Group, Department of Computer Science, University College London, Gower Street, London WC1E 6BT, UK.
authors: Domenico
authors: D
authors: Cozzetto
authors: David T
authors: DT
authors: Jones
mesh_terms: D000595:Amino Acid Sequence; D019295:Computational Biology / Q000379:methods; D030562:Databases, Protein; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D020543:Proteome; D020539:Sequence Analysis, Protein
chemical_list: D064267:Intrinsically Disordered Proteins; D020543:Proteome