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. Usin

SUBMITTER: de Brevern AG 

PROVIDER: S-EPMC7408373 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature