title: Prediction and analysis of intrinsically disordered proteins.
abstract: Intrinsically disordered proteins and protein regions (IDPs/IDRs) do not adopt a well-defined folded structure under physiological conditions. Instead, these proteins exist as heterogeneous and dynamical conformational ensembles. IDPs are widespread in eukaryotic proteomes and are involved in fundamental biological processes, mostly related to regulation and signaling. At the same time, disordered regions often pose significant challenges to the structure determination process, which generally requires highly homogeneous proteins samples. In this book chapter, we provide a brief overview of protein disorder, describe various bioinformatics resources that have been developed in recent years for their characterization, and give a general outline of their applications in various types of structural genomics projects. Traditionally, disordered segments were filtered out to optimize the yield of structure determination pipelines. However, it is becoming increasingly clear that the structural characterization of proteins cannot be complete without the incorporation of intrinsically disordered regions.
authors.affiliation: European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SD, UK.
authors.forename: Marco
authors.initials: M
authors.lastname: Punta
authors.forename: István
authors.initials: I
authors.lastname: Simon
authors.forename: Zsuzsanna
authors.initials: Z
authors.lastname: Dosztányi
mesh_terms: D003461:Crystallography / Q000295:instrumentation* / Q000379:methods; D030562:Databases, Protein; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D011487:Protein Conformation; D040901:Proteomics / Q000295:instrumentation / Q000379:methods*
chemical_list: D064267:Intrinsically Disordered Proteins