Protein disorder - function paradigm: Putative role in inflammation

Traditional protein biochemistry defends the intimate interdependence between protein function and structure, the latter being consisting of four distinct levels: premary sstructure: viz, the sequence of its constituent amino acids linked by peptides bonds - the polypeptide chain; ssecondary structure: viz, localized folding patterns (e.g., a α-helix, β-sheets) of the polypeptide chain held by hydrogen bonds between amino acid backbones; tertiary structure: viz, three-dimensional folding of the protein held by interactions between amino acid side chains mediated by disulfide bridges, hydrogen bonds, ionic bonds and hydrophobic interactions; and quaternary structure: viz, attachment of subunits, when appropriate, by means of similar chemical interactions to form a functional protein complex. Research evidence in the last decade has described intrinsically disordered proteins (IDPs) as polypeptides that lack a well-defined three/four-dimensional structure under physiological conditions, appear structurally unstable and manifest in a dynamic set of possible conformations. IDPs are a major component of the "dark" proteome, genome protein products not yet characterized through experimental structure determination and existing homology modeling. Dark proteome in general and IDPs specifically define and characterize the novel disorder - function paradigm, which critically mediate and modulate key cellular organelles and pathways and influence physiopathological processes from aging to chronic diseases and pathogen infection. The role of the disorder-function paradigm in the immunome and the inflammasome in general and specifically in the process of chronic metabolic inflammation observed in aging - i.e., inflammAging - could be elucidated through diverse AI platforms.