Protein Folding: The HP Lattice Model, Live
My roleIndependent build · lattice Monte Carlo engine, annealing schedule, and visualization
A chain of hydrophobic and polar residues folds itself on a lattice by simulated annealing, watched in real time.
Overview
An interactive implementation of Ken Dill's HP lattice model of protein folding. Each residue is either hydrophobic or polar, the chain lives on a 2D square lattice as a self-avoiding walk, and the only energy is a bonus for burying hydrophobic residues next to each other. A Metropolis Monte Carlo search over the standard lattice move set (end moves, corner flips, crankshafts), wrapped in simulated annealing, hunts for the lowest-energy fold while the hydrophobic core forms on screen. Built to understand hydrophobic collapse, energy landscapes, Levinthal's paradox, and why folding is NP-hard.
Key Features
- ✓Correct HP energy and self-avoiding-walk move set (end, corner, crankshaft)
- ✓Metropolis acceptance with a simulated-annealing temperature schedule
- ✓Live hydrophobic-core visualization and an energy-over-time trace
- ✓Grounded in the literature (Dill 1985, Anfinsen 1973, Levinthal 1969)