Document Type
Article
Publication Date
2016
Keywords
Unfolded, Flexible, Unstructured, Intrinsically Disordered, Protein Function, Structural Heterogeneity, Multi-functionality
Digital Object Identifier (DOI)
https://doi.org/10.3390/molecules21081090
Abstract
In addition to the “traditional” proteins characterized by the unique crystal-like structures needed for unique functions, it is increasingly recognized that many proteins or protein regions (collectively known as intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs)), being biologically active, do not have a specific 3D-structure in their unbound states under physiological conditions. 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 into a well-ordered functional unit or to stay intrinsically disordered but functional are encoded in the amino acid sequence. Structurally, IDPs/IDPRs are characterized by high spatiotemporal heterogeneity and exist as dynamic structural ensembles. It is important to remember, however, that although structure and disorder are often treated as binary states, they actually sit on a structural continuum.
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Molecules, v. 21, issue 8, p. 1090
Scholar Commons Citation
Deforte, Shelly and Uversky, Vladimir N., "Order, Disorder, and Everything in Between" (2016). Molecular Medicine Faculty Publications. 868.
https://digitalcommons.usf.edu/mme_facpub/868
