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.
Dates
Type | When |
---|---|
Created | 19 years, 3 months ago (May 31, 2006, 8:01 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 1:13 p.m.) |
Indexed | 1 day, 7 hours ago (Aug. 30, 2025, 12:26 p.m.) |
Issued | 33 years, 2 months ago (June 1, 1992) |
Published | 33 years, 2 months ago (June 1, 1992) |
Published Online | 33 years, 2 months ago (June 1, 1992) |
Published Print | 33 years, 2 months ago (June 1, 1992) |
@article{Goldstein_1992, title={Optimal protein-folding codes from spin-glass theory.}, volume={89}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.89.11.4918}, DOI={10.1073/pnas.89.11.4918}, number={11}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Goldstein, R A and Luthey-Schulten, Z A and Wolynes, P G}, year={1992}, month=jun, pages={4918–4922} }