HPmodel
HPmodel, short for hydrophobic-polar model, is a simplified lattice model used to study the basic principles of protein folding. The model was introduced in 1989 by Lau and Dill and has since become a standard toy model in computational biology. In the HP model, a protein is represented as a self-avoiding walk on a regular lattice, typically two- or three-dimensional. Each monomer is labeled as hydrophobic (H) or polar (P). Consecutive monomers occupy adjacent lattice sites, while non-consecutive hydrophobic contacts that occur on neighboring sites contribute to the energy of the conformation.
The energy is usually taken as E = - (number of non-bonded HH contacts). Thus stable structures minimize
Variants and computational aspects: Most studies use a 2D square lattice; some extend to 3D cubic lattices
Significance and limitations: The HP model serves as a conceptual framework for exploring how hydrophobicity drives