Optimal protein-folding codes from spin-glass theory.

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.

SUBMITTER: Goldstein RA 

PROVIDER: S-EPMC49199 | biostudies-other | 1992 Jun

REPOSITORIES: biostudies-other