Denaturant-induced Conformational Transitions in Intrinsically Disordered Proteins
Conformational Stability, Denaturant-induced Unfolding, Molten Globule, Pre-molten Globule, Two-state Transition, Three-state Transition
Digital Object Identifier (DOI)
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.
Was this content written or created while at USF?
Citation / Publisher Attribution
Denaturant-Induced Conformational Transitions in Intrinsically Disordered Proteins, in V. N. Uversky & A. K. Dunker (Eds.), Intrinsically Disordered Protein Analysis, Springer, p. 197-213
Scholar Commons Citation
Neyroz, Paolo; Ciurli, Stefano; and Uversky, Vladimir N., "Denaturant-induced Conformational Transitions in Intrinsically Disordered Proteins" (2012). Molecular Medicine Faculty Publications. 1061.