title: 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.
authors.affiliation: School of Chemical Sciences, University of Illinois, Urbana 61801.
authors.forename: R A
authors.initials: RA
authors.lastname: Goldstein
authors.forename: Z A
authors.initials: ZA
authors.lastname: Luthey-Schulten
authors.forename: P G
authors.initials: PG
authors.lastname: Wolynes
mesh_terms: D001536:Bence Jones Protein / Q000648:ultrastructure; D003461:Crystallography; D004268:DNA-Binding Proteins; D006801:Humans; D066298:In Vitro Techniques; D008958:Models, Molecular; D008962:Models, Theoretical; D011487:Protein Conformation; D012097:Repressor Proteins / Q000648:ultrastructure; D012995:Solubility; D013816:Thermodynamics; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; D014867:Water
chemical_list: D004268:DNA-Binding Proteins; D012097:Repressor Proteins; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins; D014867:Water; D001536:Bence Jones Protein