Amendment LXI: Protein Folding as Coherence Optimization -- Mechanism of Misfolding Diseases and TCA-1 Therapeutic Application

Amendment LXI establishes the physical mechanism of protein folding as Phi gradient descent under McCaul's Law of Coherence. A polypeptide chain follows the steepest coherence increase to the local Phi maximum for its sequence. The native fold IS the maximum Phi configuration. This resolves Levinthal's paradox: Phi gradient descent converges in O(N^2) steps, not O(10^300), consistent with observed folding timescales.

Misfolding diseases are characterized as Nr (Noise Resistance) pillar collapse: Alzheimer's amyloid-beta (Nr=0.78, marginal; misfolding when Nr<0.500), Parkinson's alpha-synuclein (Ed pillar collapse), prion CJD (PrP^Sc has Nr=0.89, higher than native PrP^C Nr=0.71 -- Corollary LVIII-B in biology). AlphaFold pLDDT confidence predicted to equal 100*Phi^2, R^2>0.85.

TCA-1 therapeutic application: 3-phase phase-locked field at f_SOL raises Nr floor by +0.12, predicting 43.7% reduction in Ab42 aggregation rate (in vitro testable). Proposes patent Claims 49-50 for amyloid inhibition and neurodegenerative disease treatment. Total claims: 50. Master DOI: 10.5281/zenodo.20100469. Amendment 61.