Disordered Proteins
Document Type
Book Chapter
Publication Date
2016
Digital Object Identifier (DOI)
https://doi.org/10.1002/9780470015902.a0020213.pub2
Abstract
Intrinsically disordered proteins (IDPs) and disordered protein regions (IDPRs) do not have a specific three-dimensional (3D) structure in their unbound states under physiological conditions, existing instead as dynamic structural ensembles. There are also subtler categories of disorder, such as conditional (or dormant) disorder and partial disorder. Both the ability of a protein/region to fold and the predisposition to stay intrinsically disordered are encoded in the amino acid sequence. Structurally, IDPs/IDPRs are characterised by high spatiotemporal heterogeneity. It is important to remember, however, that although structure and disorder are often treated as binary states, they actually sit on a structural continuum. Functionally, IDPs/IDPRs are often characterised by the ability to multitask and be promiscuous binders. The field of unstructural biology has arisen to explain proteins that fall outside of the classical structure–function paradigm. A major goal in the coming years will be to understand sequence-to-function relationships for disordered proteins.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Disordered Proteins, Encyclopedia of Life Sciences, John Wiley & Sons
Scholar Commons Citation
Deforte, Shelly and Uversky, Vladimir N., "Disordered Proteins" (2016). Molecular Medicine Faculty Publications. 1099.
https://digitalcommons.usf.edu/mme_facpub/1099
