Protein folding as a configurational reconstruction: Bio-epistemic application of the General Epistemic Dispersion Theory to adult human hemoglobin

This manuscript proposes a theoretical application of the General Epistemic Dispersion Theory (GEDT) to the domain of molecular biology, utilizing adult human hemoglobin (HbA) as a model study. The work formalizes protein folding as a configurational reconstruction problem, investigating how informational load is partitioned between structural constraints and dynamic assistance. The study introduces a conditional decomposition of configurational uncertainty, H(Π | F) = I(Π ; S | F) + H(Π | F, S), mapping the primary amino acid sequence to the structural core (S) and the physicochemical environment to the finite space of feasible configurations (𝒫). Through the comparative analysis of HbA assembly, the role of the Alpha-Hemoglobin Stabilizing Protein (AHSP), and specific variants (HbS and Hb G-Copenhagen), the paper examines the informational boundaries of spontaneous folding and dynamic chaperone intervention. This preprint does not introduce novel biochemical mechanisms nor present new experimental biological data.The primary objective is to establish a falsifiable and operationalizable informational framework to quantify the residual configurational uncertainty in biological systems, offering a purely epistemic perspective on the structural economy of molecular folding.