title: Intrinsic disorder and functional proteomics.
abstract: The recent advances in the prediction of intrinsically disordered proteins and the use of protein disorder prediction in the fields of molecular biology and bioinformatics are reviewed here, especially with regard to protein function. First, a close look is taken at intrinsically disordered proteins and then at the methods used for their experimental characterization. Next, the major statistical properties of disordered regions are summarized, and prediction models developed thus far are described, including their numerous applications in functional proteomics. The future of the prediction of protein disorder and the future uses of such predictions in functional proteomics comprise the last section of this article.
authors.affiliation: School of Informatics, Indiana University, Bloomington, Indiana, USA.
authors.forename: Predrag
authors.initials: P
authors.lastname: Radivojac
authors.forename: Lilia M
authors.initials: LM
authors.lastname: Iakoucheva
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Oldfield
authors.forename: Zoran
authors.initials: Z
authors.lastname: Obradovic
authors.forename: Vladimir N
authors.initials: VN
authors.lastname: Uversky
authors.forename: A Keith
authors.initials: AK
authors.lastname: Dunker
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D019295:Computational Biology; D003627:Data Interpretation, Statistical; D030562:Databases, Protein; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry* / Q000502:physiology; D040901:Proteomics / Q000379:methods*
chemical_list: D011506:Proteins