title: Denaturant-induced conformational transitions in intrinsically disordered proteins.
abstract: Intrinsically disordered proteins (IDPs) differ from ordered proteins at several levels: structural, functional, and conformational. Amino acid biases also drive atypical responses of IDPs to changes in their environment. Among several specific features, the conformational behavior of IDPs is characterized by the low cooperativity (or the complete lack thereof) of the denaturant-induced unfolding. In fact, the denaturant-induced unfolding of native molten globules can be described by shallow sigmoidal curves, whereas urea- or guanidinium hydrochloride-induced unfolding of native pre-molten globules or native coils is a noncooperative process and typically is seen as monotonous feature-less changes in the studied parameters. This chapter describes some of the most characteristic features of the IDP conformational behavior.
authors: Dipartimento di Biochimica "G. Moruzzi", Università di Bologna, Via San Donato, Bologna, Italy.
authors: Paolo
authors: P
authors: Neyroz
authors: Stefano
authors: S
authors: Ciurli
authors: Vladimir N
authors: VN
authors: Uversky
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification; D002850:Chromatography, Gel; D019791:Guanidine / Q000494:pharmacology; D028044:Phosphate-Binding Proteins; D011487:Protein Conformation / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects*; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification; D013050:Spectrometry, Fluorescence
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D028044:Phosphate-Binding Proteins; D011506:Proteins; C082270:ureG protein, Bacteria; D019791:Guanidine