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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1992 Jun 1;89(11):4918–4922. doi: 10.1073/pnas.89.11.4918

Optimal protein-folding codes from spin-glass theory.

R A Goldstein 1, Z A Luthey-Schulten 1, P G Wolynes 1
PMCID: PMC49199  PMID: 1594594

Abstract

Protein-folding codes embodied in sequence-dependent energy functions can be optimized using spin-glass theory. Optimal folding codes for associative-memory Hamiltonians based on aligned sequences are deduced. A screening method based on these codes correctly recognizes protein structures in the "twilight zone" of sequence identity in the overwhelming majority of cases. Simulated annealing for the optimally encoded Hamiltonian generally leads to qualitatively correct structures.

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Selected References

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