title: Conformational disorder.
abstract: In recent years it was shown that a large number of proteins are either fully or partially disordered. Intrinsically disordered proteins are ubiquitary proteins that fulfill essential biological functions while lacking a stable 3D structure. Despite the large abundance of disorder, disordered regions are still poorly detected. The identification of disordered regions facilitates the functional annotation of proteins and is instrumental in delineating boundaries of protein domains amenable to crystallization. This chapter focuses on the methods currently employed for predicting disorder and identifying regions involved in induced folding.
authors.affiliation: Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Universités Aix-Marseille I et II, Marseille, France.
authors.forename: Sonia
authors.initials: S
authors.lastname: Longhi
authors.forename: Philippe
authors.initials: P
authors.lastname: Lieutaud
authors.forename: Bruno
authors.initials: B
authors.lastname: Canard
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D019295:Computational Biology; D057225:Data Mining; D030562:Databases, Protein; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D020539:Sequence Analysis, Protein; D013329:Structure-Activity Relationship
chemical_list: D011506:Proteins