Pre-dynamical ordering in protein folding via the Nomadic Principle

This preprint introduces a non-iterative, kernel-based framework for protein folding inspired by the Nomadic Principle. Instead of treating folding as a stochastic dynamical search, we show that major structural features—hydrophobic cores and long-range tertiary contacts—can be recovered directly from the amino-acid sequence using a single convolution with a fixed solvent-response kernel. A fully reproducible reference implementation has been uploaded alongside this manuscript. The code reproduces all figures and quantitative results presented in the paper, including coherence-length discovery, contact-map enrichment, and a negative control. The implementation is deterministic, physics-based, and requires no training data or molecular dynamics simulation. The code is intended as a proof-of-principle and high-throughput screening tool, not as a replacement for atomistic folding simulations.