This application enumerates and calculates equilibrium populations for all possible conformations of model peptides between 1 and 15 residues on a two-dimensional (2D) lattice. The peptides can be composed of any sequence of four simplified amino acids A, E, K, and P with the simplified properties:

• A is hydrophobic: A favorable energy shift is applied for each direct A-A contact. 
• E is negatively charged: A favorable energy shift is applied for E-K contacts, and a disfavorable shift for E-E contacts.
• K is positively charged: A favorable energy shift is applied for K-E contacts, and a disfavorable shift for K-K contacts. 
• P is sterically constrained: A favorable shift is applied for right-hand turns and a disfavorable shift for left-hand turns. No offset is applied for straight conformations. 

Researchers should cite this work as follows:

• Michael Earl Reppert (2022), "Two-dimensional Lattice Protein Simulator," https://nanohub.org/resources/latticeprotein. (DOI: 10.21981/J26R-N216).

  BibTex | EndNote

1. 2D Lattice Protein Simulator
2. Lattice polymer
3. Lattice Protein
4. protein folding