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Analysis of Protein Disorder Predictions in the Light of a Protein Structural Alphabet

Abstract : Intrinsically-disordered protein (IDP) characterization was an amazing change of paradigm in our classical sequence-structure-function theory. Moreover, IDPs are over-represented in major disease pathways and are now often targeted using small molecules for therapeutic purposes. This has had created a complex continuum from order-that encompasses rigid and flexible regions-to disorder regions; the latter being not accessible through classical crystallographic methodologies. In X-ray structures, the notion of order is dictated by access to resolved atom positions, providing rigidity and flexibility information with low and high experimental B-factors, while disorder is associated with the missing (non-resolved) residues. Nonetheless, some rigid regions can be found in disorder regions. Using ensembles of IDPs, their local conformations were analyzed in the light of a structural alphabet. An entropy index derived from this structural alphabet allowed us to propose a continuum of states from rigidity to flexibility and finally disorder. In this study, the analysis was extended to comparing these results to disorder predictions, underlying a limited correlation, and so opening new ideas to characterize and predict disorder.
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Submitted on : Monday, July 27, 2020 - 3:30:48 PM
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Alexandre de Brevern. Analysis of Protein Disorder Predictions in the Light of a Protein Structural Alphabet. Biomolecules, MDPI, 2020, 10 (7), pp.1080. ⟨10.3390/biom10071080⟩. ⟨inserm-02907391⟩



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