The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Tryptophan zippers: Stable, monomeric β-hairpins
Open accessAbstract
A structural motif, the tryptophan zipper (trpzip), greatly stabilizes the β-hairpin conformation in short peptides. Peptides (12 or 16 aa in length) with four different turn sequences are monomeric and fold cooperatively in water, as has been observed previously for some hairpin peptides. However, the folding free energies of the trpzips exceed substantially those of all previously reported β-hairpins and even those of some larger designed proteins. NMR structures of three of the trpzip peptides reveal exceptionally well-defined β-hairpin conformations stabilized by cross-strand pairs of indole rings. The trpzips are the smallest peptides to adopt an unique tertiary fold without requiring metal binding, unusual amino acids, or disulfide crosslinks.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Cited by
Designing a 20-residue protein
Neidigh, J. W., Fesinmeyer, R. M., & Andersen, N. H. (2002) · Nature Structural Biology · doi:10.1038/nsb798 · Cited by 793
Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
Richardson, J. S., & Richardson, D. C. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052706099 · Cited by 753
Marzec, M., Eletto, D., & Argon, Y. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.10.013 · Cited by 390
β-Hairpin Peptidomimetics: Design, Structures and Biological Activities
Robinson, J. A. (2008) · Accounts of Chemical Research · doi:10.1021/ar700259k · Cited by 321
Lien, S., & Lowman, H. B. (2003) · Trends in Biotechnology · doi:10.1016/j.tibtech.2003.10.005 · Cited by 209
Metadata
- Authors
- Cochran, A. G., Skelton, N. J., & Starovasnik, M. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2001-05
- Volume
- 98
- Issue
- 10
- Pages
- 5578-5583
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2103072162
- Cited by
- 735
- References
- 1
- FWCI
- 7.17
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Tryptophan zippers: Stable, monomeric β-hairpins. https://app.cochat.ai/papers/10.1073/pnas.091100898
- The paper
- Cochran, A. G., Skelton, N. J., & Starovasnik, M. A. (2001). Tryptophan zippers: Stable, monomeric β-hairpins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.091100898
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.
