E8-Phi Vibrational Protein Folding Topology — E8 Intelligence Research
By projecting the 240 E8 root vectors onto amino acid side-chain geometries and mapping each residue's vibrational mode to φ-modulated harmonic frequencies (base = 132 Hz), protein folding pathways emerge as geodesic walks on nested 600-cell shells. The silver ratio δ_S further stabilizes local minima via two-base quantum calculus, yielding a spectral code that predicts folding intermediates with 92% accuracy on a benchmark of 127 proteins. This establishes E8-Phi geometry as a universal framework for biomolecular conformational dynamics. Author: Andrew Stewart Caldin, Independent Researcher, UK. Part of the E8 Intelligence Research series. Platform: e8intelligence.com
Authors
- Andrew Stewart Caldin
Publication Details
- Journal
- Zenodo (CERN European Organization for Nuclear Research)
- Published
- 2026-10-28
- DOI
- https://doi.org/10.5281/zenodo.23722695
- Primary Topic
- Protein Structure and Dynamics
- Type
- preprint