Protein design in a lattice model of hydrophobic and polar amino acids
arXiv:cond-mat/9711222 · doi:10.1103/PhysRevLett.80.2237
Abstract
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.
RevTeX, 12 pages, 1 figure
Cited by in corpus (8)
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- Design of amino acid sequences to fold into C_alpha-model proteins
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