QAOA Protein Folding — a true 3D lattice walk
This is the genuine three-dimensional companion of the 2D QAOA protein-folding visualization: the same hydrophobic-polar (HP) lattice model — Dill, 1985 — and the same conceptual QAOA cost/mixer circuit pipeline, but the backbone conformation is now a real self-avoiding walk on a 3D cubic lattice (six possible turn directions per bond instead of four), rendered with genuine WebGL depth and a free-orbit camera instead of a flat canvas projection. Hydrophobic (H, orange) and polar (P, blue) residues are placed by the same coarse-graining rule; non-adjacent H residues that land on lattice-neighboring cells form the favorable H-H contacts (yellow, pulsing) whose count sets the HP energy, exactly as in the classic Dill formulation and its turn-encoded QAOA implementations (e.g. Robert et al. 2021, npj Quantum Information).
Drag to orbit, scroll or pinch to zoom. The QAOA Depth slider changes the number of alternating cost/mixer layers shown in the circuit panel and used in the gate-count estimate; the Chain Length slider reseeds a new self-avoiding walk of that many residues; Reseed draws a fresh random fold without changing length; Orbit Speed adds continuous auto-rotation.