Phys. Rev. Lett. 80, p. 2237-2240 (1998).
Protein Design in a Lattice Model of Hydrophobic and Polar Amino Acids
Cristian Micheletti, Flavio Seno, Amos Maritan, and Jayanth R. Banavar
Link to online article.
A general strategy is described for finding which amino acid sequences
have native states in a desired conformation (inverse design). The
approach is used to design sequences of 48 hydrophobic and polar amino
acids on three-dimensional lattice structures. Previous studies
employing a sequence-space Monte Carlo technique resulted in the
successful design of one sequence in ten attempts. The present work
also entails the exploration of conformations that compete
significantly with the target structure for being its ground
state. The design procedure is successful in all the ten cases.