A chain of thirteen residues, each hydrophobic or polar, folds in the plane. The bend angle at each interior residue sets the shape, and the energy rewards a compact hydrophobic core while polar and mixed contacts cost more. It is the textbook extreme-multimodality benchmark (Stillinger's 2D AB model): an enormous forest of local minima around the true fold. Score is total energy, to minimise. 11-D.
| Algorithm | Energy | Evals |
|---|---|---|
| — no runs yet — | ||
The JS objective is a line-for-line port of
example_applications/protein_fold_toy and agrees to floating-point
tolerance. Filled dots are hydrophobic residues, hollow dots polar; good folds bury
the filled ones together in a compact core.