The DOI matches its Crossref record.
Design of a Monomeric 23-Residue Polypeptide with Defined Tertiary Structure
Abstract
Small proteins or protein domains generally require disulfide bridges or metal sites for their stabilization. Here it is shown that the ββα architecture of zinc fingers can be reproduced in a 23-residue polypeptide in the absence of metal ions. The sequence was obtained through an iterative design process. A key feature of the final design is the incorporation of a type II' β turn to aid in β-hairpin formation. Nuclear magnetic resonance analysis reveals that the α helix and β hairpin are held together by a defined hydrophobic core. The availability of this structural template has implications for the development of functional polypeptides.
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
Cited by
De Novo Design of Helical Bundles as Models for Understanding Protein Folding and Function
Hill, R. B., Raleigh, D. P., Lombardi, A., & DeGrado, W. F. (2000) · Accounts of Chemical Research · doi:10.1021/ar970004h · Cited by 300
Rationally designed mutations convert de novo amyloid-like fibrils into monomeric β-sheet proteins
Wang, W., & Hecht, M. H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052706199 · Cited by 159
Rua, A. J., & Alexandrescu, A. T. (2024) · Protein Science · doi:10.1002/pro.5149 · Cited by 5
Metadata
- Authors
- Struthers, M. D., Cheng, R. P., & Imperiali, B.
- Venue
- Science
- Published
- 1996-01-19
- Volume
- 271
- Issue
- 5247
- Pages
- 342-345
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2161164474
- Cited by
- 300
- References
- 0
- FWCI
- 10.89
- Type
- journal article
- Language
- en
- Open access
- closed
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: Design of a Monomeric 23-Residue Polypeptide with Defined Tertiary Structure. https://app.cochat.ai/papers/10.1126/science.271.5247.342
- The paper
- Struthers, M. D., Cheng, R. P., & Imperiali, B. (1996). Design of a Monomeric 23-Residue Polypeptide with Defined Tertiary Structure. Science. https://doi.org/10.1126/science.271.5247.342
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.
