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. 2013 Sep 3;21(9):1492-9.
doi: 10.1016/j.str.2013.08.001.

From sequence and forces to structure, function, and evolution of intrinsically disordered proteins

Julie D Forman-Kay  1 , Tanja Mittag
Affiliations

From sequence and forces to structure, function, and evolution of intrinsically disordered proteins

Julie D Forman-Kay et al. Structure. .

Abstract

Intrinsically disordered proteins (IDPs), which lack persistent structure, are a challenge to structural biology due to the inapplicability of standard methods for characterization of folded proteins as well as their deviation from the dominant structure/function paradigm. Their widespread presence and involvement in biological function, however, has spurred the growing acceptance of the importance of IDPs and the development of new tools for studying their structure, dynamics, and function. The interplay of folded and disordered domains or regions for function and the existence of a continuum of protein states with respect to conformational energetics, motional timescales, and compactness are shaping a unified understanding of structure-dynamics-disorder/function relationships. In the 20(th) anniversary of Structure, we provide a historical perspective on the investigation of IDPs and summarize the sequence features and physical forces that underlie their unique structural, functional, and evolutionary properties.

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Figures

Figure 1
Figure 1
Summary of characteristics of intrinsically disordered proteins and regions (IDPs/IDRs) as an inter-related set rooted in their sequence features and physical forces dominating their interactions and continuing through their structural, functional and evolutionary properties. Posttranslational modifications; PTMs.
See this image and copyright information in PMC

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