Phys. Rev. Lett. 80, 5683-5686, (1998).
Steric Constraints in Model Proteins
Cristian Micheletti, Jayanth R. Banavar, Amos Maritan and Flavio Seno
Link to online article.
A simple lattice model for proteins that allows for distinct sizes of
the amino acids is presented. The model is found to lead to a
significant number of encodable conformations that are the unique
ground state of one or more sequences. Furthermore, several of the
encodable structures are highly designable and are the nondegenerate
ground state of several sequences. Even though the native state
conformations are typically compact, not all compact conformations are
encodable. The incorporation of the hydrophobic and polar nature of
amino acids further enhances the attractive features of the model.