Protein design in a lattice model of hydrophobic and polar amino acids

Details Protein design in a lattice model of hydrophobic and polar amino acids Protein design in a lattice model of hydrophobic and polar amino acids

1997-11-21

arxiv.org/abs/cond-mat/9711222v1

Physics

Condensed Matter

Statistical Mechanics

RevTeX, 12 pages, 1 figure

Scientific paper

10.1103/PhysRevLett.80.2237

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 aminoacids 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.

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