Optimal protein-folding codes from spin-glass theory

Richard A. Goldstein, Zaida A. Luthey-Schulten, Peter G. Wolynes

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)4918-4922
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number11
StatePublished - 1992


  • Associative memories
  • Biomolecular dynamics
  • Neural networks
  • Protein-structure prediction

ASJC Scopus subject areas

  • General


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