A structural entropy index to analyse local conformations in intrinsically disordered proteins - Inserm - Institut national de la santé et de la recherche médicale
Journal Articles Journal of Structural Biology Year : 2020

A structural entropy index to analyse local conformations in intrinsically disordered proteins

Narayanaswamy Srinivasan
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Abstract

Sequence – structure – function paradigm has been revolutionized by the discovery of disordered regions and disordered proteins more than two decades ago. While the definition of rigidity is simple with X-ray structures, the notion of flexibility is linked to high experimental B-factors. The definition of disordered regions is more complex as in these same X-ray structures; it is associated to the position of missing residues. Thus a continuum so seems to exist between rigidity, flexibility and disorder. However, it had not been precisely described. In this study, we used an ensemble of disordered proteins (or regions) and, we applied a structural alphabet to analyse their local conformation. This structural alphabet, namely Protein Blocks, had been efficiently used to highlight rigid local domains within flexible regions and so discriminates deformability and mobility concepts. Using an entropy index derived from this structural alphabet, we underlined its interest to measure these local dynamics, and to quantify, for the first time, continuum states from rigidity to flexibility and finally disorder. We also highlight non-disordered regions in the ensemble of disordered proteins in our study.
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Dates and versions

inserm-02907335 , version 1 (27-07-2020)

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Akhila Melarkode Vattekatte, Tarun Jairaj Narwani, Aline Floch, Mirjana Maljković, Soubika Bisoo, et al.. A structural entropy index to analyse local conformations in intrinsically disordered proteins. Journal of Structural Biology, 2020, 210 (1), pp.107464. ⟨10.1016/j.jsb.2020.107464⟩. ⟨inserm-02907335⟩
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