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Cited by 220

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Protein tertiary structure recognition using optimized Hamiltonians with local interactions.

Open access
Goldstein, R A, Luthey-Schulten, Z A, Wolynes, P G·1992·Proceedings of the National Academy of Sciences

Abstract

Protein folding codes embodying local interactions including surface and secondary structure propensities and residue-residue contacts are optimized for a set of training proteins by using spin-glass theory. A screening method based on these codes correctly matches the structure of a set of test proteins with proteins of similar topology with 100% accuracy, even with limited sequence similarity between the test proteins and the structural homologs and the absence of any structurally similar proteins in the training set.

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Crossref · 10.1073/pnas.89.19.9029

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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
1992-10
Volume
89
Issue
19
Pages
9029-9033
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1998072661
Cited by
220
References
4
FWCI
4.58
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Protein tertiary structure recognition using optimized Hamiltonians with local interactions. https://app.cochat.ai/papers/10.1073/pnas.89.19.9029
The paper
Goldstein, R. A., Luthey-Schulten, Z. A., & Wolynes, P. G. (1992). Protein tertiary structure recognition using optimized Hamiltonians with local interactions. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.19.9029

Data sources

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).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.