Document Type

Article

Publication Date

2016

Keywords

intrinsically disordered protein, multifunctional protein, post-translational modification (PTM), protein folding, protein-protein interaction, complexity, dynamical system, structural heterogeneity, intrinsically disordered proteins, posttranslational modification

Digital Object Identifier (DOI)

https://doi.org/10.1074/jbc.R115.685859

Abstract

Biologically active but floppy proteins represent a new reality of modern protein science. These intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered and intrinsically disordered protein regions (IDPRs) constitute a noticeable part of any given proteome. Functionally, they complement ordered proteins, and their conformational flexibility and structural plasticity allow them to perform impossible tricks and be engaged in biological activities that are inaccessible to well folded proteins with their unique structures. The major goals of this minireview are to show that, despite their simplified amino acid sequences, IDPs/IDPRs are complex entities often resembling chaotic systems, are structurally and functionally heterogeneous, and can be considered an important part of the structure-function continuum. Furthermore, IDPs/IDPRs are everywhere, and are ubiquitously engaged in various interactions characterized by a wide spectrum of binding scenarios and an even wider spectrum of structural and functional outputs.

Rights Information

Creative Commons License
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

Journal of Biological Chemistry, v. 291, issue 13, p. 6681-6688

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