Modeling Protein Folding with a Fractal Wave Function
Protein folding is one of biophysics’ most complex problems, and the classical approach describes this process as a minimization problem on a multidimensional free energy landscape. This study reformulates protein folding within the Fractal Mechanics (FM) framework, modeling the folding process as a spiral–hierarchical collapse of a fractal wave function. The proposed model defines a local spiral wave number (k-local) for each amino acid and a hierarchical resonance parameter (q) for each structural scale, suggesting that folding is driven not only by energy but also by resonance and fractal continuity. Comparative analysis with the classical funnel model shows that FM offers novel advantages, particularly in explaining rapid folding, misfolding, and aggregation phenomena.








