The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
A designed beta-hairpin peptide in crystals.
Open accessAbstract
Beta-hairpin structures have been crystallographically characterized only in very short acyclic peptides, in contrast to helices. The structure of the designed beta-hairpin, t-butoxycarbonyl-Leu-Val-Val-D-Pro-Gly-Leu-Val-Val-OMe in crystals is described. The two independent molecules of the octapeptide fold into almost ideal beta-hairpin conformations with the central D-Pro-Gly segment adopting a Type II' beta-turn conformation. The definitive characterization of a beta-hairpin has implications for de novo peptide and protein design, particularly for the development of three- and four-stranded beta-sheets.
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Cites
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a001 · Cited by 2,172
Cited by
Vasudev, P. G., Chatterjee, S., Shamala, N., & Balaram, P. (2011) · Chemical Reviews · doi:10.1021/cr100100x · Cited by 329
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Metadata
- Authors
- Karle, I. L., Awasthi, S. K., & Balaram, P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1996-08-06
- Volume
- 93
- Issue
- 16
- Pages
- 8189-8193
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2073295365
- Cited by
- 174
- References
- 1
- FWCI
- 2.23
- Type
- journal article
- Language
- en
- Open access
- green
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- Karle, I. L., Awasthi, S. K., & Balaram, P. (1996). A designed beta-hairpin peptide in crystals. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.93.16.8189
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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.
