Riedel-Teichmüller Protein Folding Hypothesis

Protein folding remains a central challenge in biology, where geometric insight and physical constraints must align. This work introduces a conceptual framework that applies quasi-conformal maps, Riemannian geometry, and rotation matrices to model folding dynamics in terms of psi, phi, and omega backbone angles. By incorporating electronegativity gradients and bond-length constraints into topological structures, the hypothesis aims to connect quantum-level interactions with macroscopic conformational transitions. Rather than presenting a finalized model, this proposal outlines a starting point for interdisciplinary collaboration. From potentially GPU accelerated optimization of quasi-conformalmaps to potential applications in moduli space analysis, the approach invites contributions from mathematics, biophysics, and computational science. Though preliminary, the hypothesis is intended as a scaffold for further development, a shared effort to explore new directions in protein modeling.