Open AccessOptimal protein-folding codes from spin-glass theory.
Author(s) -
Richard A. Goldstein,
Zaida LutheySchulten,
Peter G. Wolynes
Publication year - 1992
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.89.11.4918
Subject(s) - sequence (biology) , protein folding , hamiltonian (control theory) , folding (dsp implementation) , physics , computer science , computational biology , algorithm , mathematics , biology , genetics , engineering , mathematical optimization , nuclear magnetic resonance , electrical engineering
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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