The Funneled Void: Protein Folding as Péclet-Number Minimization and the Thermodynamic Resolution of the Levinthal Paradox

Formalizes protein folding as a Péclet-number minimization process. The Levinthal paradox (3^100 conformational states) is resolved by showing the funneled energy landscape is the physical implementation of the prohibition-ritual pair: the funnel IS the constraint specification. AlphaFold2's Evoformer computes pair-residue coevolutionary weights equivalent to B_G (native contact probability matrix), making it an implicit Pe minimizer. Empirical test: ρ(Pe_agg, aggregation_propensity) > 0.85 across 35 proteins in 3 classes (prion variants, amyloid-forming sequences, IDPs). Results: Class 1 ρ=1.000, Class 2 ρ=0.909, Class 3 ρ=0.936, Pooled ρ=0.972. Falsification test: rat IAPP (non-amyloidogenic) has Pe_agg < 0, human IAPP Pe_agg = 16.0.