The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Optimal protein-folding codes from spin-glass theory.
Open accessAbstract
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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Cites
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A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional Structure
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Self-citationLüthy, R., McLachlan, A. D., & Eisenberg, D. (1991) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340100307 · Cited by 167
Toward Protein Tertiary Structure Recognition by Means of Associative Memory Hamiltonians
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Self-citationA search for the most stable folds of protein chains
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[6] Searching through sequence databases
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Cited by
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648
“In addition, molecular dynamics calculations using associative memory Hamiltonians optimized in this way reliably gave native-like structures [83, 84].”
BackgroundSelf-citationTHEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
Onuchic, J. N., Luthey-Schulten, Z., & Wolynes, P. G. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.545 · Cited by 2,210
Self-citationPerspective: Coarse-grained models for biomolecular systems
Noid, W. G. (2013) · The Journal of Chemical Physics · doi:10.1063/1.4818908 · Cited by 893
Toward an outline of the topography of a realistic protein-folding funnel.
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Self-citationFerreiro, D. U., Komives, E. A., & Wolynes, P. G. (2014) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583514000092 · Cited by 314
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Metadata
- Authors
- Goldstein, R. A., Luthey-Schulten, Z. A., & Wolynes, P. G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1992-06
- Volume
- 89
- Issue
- 11
- Pages
- 4918-4922
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2060792417
- Cited by
- 344
- References
- 12
- FWCI
- 3.82
- Type
- journal article
- Language
- en
- Open access
- green
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- Goldstein, R. A., Luthey-Schulten, Z. A., & Wolynes, P. G. (1992). Optimal protein-folding codes from spin-glass theory. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.11.4918
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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