Intrinsically disordered proteins (IDP) appear far more likely to engage in functional moonlighting than well-structured proteins. The recent use of nonrigid molecule theory to address IDP structure and dynamics produces this result directly: mirror image subgroup or subgroupoid tiling matching of the molecular fuzzy lock-and-key can be much richer for IDP's since the number of possible group or groupoid symmetries can grow exponentially with molecule length, while tiling matching for 3D structured proteins is relatively limited. An 'information catalysis' model suggests how this mechanism can produce a vast spectrum of biological logic gates having subtle properties far beyond familiar AND, OR, XOR, etc. behaviors. Inferring the general from the particular, the analysis adds weight to arguments that a fundamental defining characteristic of the living state is the operation of chemical or other cognitive processes at virtually every scale and level of organization. © 2011 Académie des sciences. Published by Elsevier Masson SAS. All rights reserved.
Wallace, R. (2011). Multifunction moonlighting and intrinsically disordered proteins: Information catalysis, non-rigid molecule symmetries and the “logic gate” spectrum. Comptes Rendus Chimie, 14(12), 1117–1121. https://doi.org/10.1016/j.crci.2011.10.003