Paradoxes and Wonders of Intrinsic Disorder: Stability of Instability

Document Type

Article

Publication Date

2017

Keywords

conformational stability, intrinsically disordered protein, liquid-liquid phase transition, membrane-less organelle, protein-protein interaction

Digital Object Identifier (DOI)

https://doi.org/10.1080/21690707.2017.1327757

Abstract

This article continues a series of short comments on the paradoxes and wonders of the protein intrinsic disorder phenomenon by introducing the “stability of instability” paradox. Intrinsically disordered proteins (IDPs) are characterized by the lack of stable 3D-structure, and, as a result, have an exceptional ability to sustain exposure to extremely harsh environmental conditions (an illustration of the “you cannot break what is already broken” principle). Extended IDPs are known to possess extreme thermal and acid stability and are able either to keep their functionality under these extreme conditions or to rapidly regain their functionality after returning to the normal conditions. Furthermore, sturdiness of intrinsic disorder and its capability to “ignore” harsh conditions provides some interesting and important advantages to its carriers, at the molecular (e.g., the cell wall-anchored accumulation-associated protein playing a crucial role in intercellular adhesion within the biofilm of Staphylococcus epidermidis), supramolecular (e.g., protein complexes, biologic liquid-liquid phase transitions, and proteinaceous membrane-less organelles), and organismal levels (e.g., the recently popularized case of the microscopic animals, tardigrades, or water bears, that use intrinsically disordered proteins to survive desiccation).

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Citation / Publisher Attribution

Intrinsically Disordered Proteins, v. 5, issue 1, art. e1327757

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