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Cited by 1,375

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential

Open access
Bahar, Ivet, Atilgan, Ali Rana, Erman, Burak·1997·Folding and Design
DOI 10.1016/s1359-0278(97)00024-2
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Citations

Cites

  • LINUS: a hierarchic procedure to predict the fold of a protein

    Srinivasan, R., & Rose, G. D. (1995) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340220202 · Cited by 266 · cited 1×

    “On the other hand, some recent studies have suggested that simple energy functions that incorporate the two most important characteristics of amino acids, mainly hydrophobicity and hydrogen bond formation capacity, may adequately account for the selection of some supersecondary structures or tertiary folds in small pr…”
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Metadata

Authors
Bahar, I., Atilgan, A. R., & Erman, B.
Venue
Folding and Design
Publisher
Elsevier BV
Published
1997-06
Volume
2
Issue
3
Pages
173-181
ISSN
1359-0278 (ISSN-L)
DOI
10.1016/s1359-0278(97)00024-2
OpenAlex
W2101017457
Cited by
1,375
References
1
FWCI
3.49
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. https://app.cochat.ai/papers/10.1016/s1359-0278(97)00024-2
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Bahar, I., Atilgan, A. R., & Erman, B. (1997). Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Folding and Design. https://doi.org/10.1016/s1359-0278(97)00024-2

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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).

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