The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Structure at 2.5 Å of a Designed Peptide that Maintains Solubility of Membrane Proteins
Abstract
A 24-amino acid peptide designed to solubilize integral membrane proteins has been synthesized. The design was for an amphipathic α helix with a "flat" hydrophobic surface that would interact with a transmembrane protein as a detergent. When mixed with peptide, 85 percent of bacteriorhodopsin and 60 percent of rhodopsin remained in solution over a period of 2 days in their native forms. The crystal structure of peptide alone showed it to form an antiparallel four-helix bundle in which monomers interact, flat surface to flat surface, as predicted.
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
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578
Cited by
Detergents for the stabilization and crystallization of membrane proteins
Privé, G. G. (2007) · Methods · doi:10.1016/j.ymeth.2007.01.007 · Cited by 532
Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions
Tribet, C., Audebert, R., & Popot, J.-L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15047 · Cited by 473
Engineering Escherichia coli for production of functionalized terpenoids using plant P450s
Chang, M. C. Y., Eachus, R. A., Trieu, W., Ro, D.-K., & Keasling, J. D. (2007) · Nature Chemical Biology · doi:10.1038/nchembio875 · Cited by 364
A saposin-lipoprotein nanoparticle system for membrane proteins
Frauenfeld, J., Löving, R., Armache, J.-P., Sonnen, A. F.-P., Guettou, F., Moberg, P., Zhu, L., Jegerschöld, C., Flayhan, A., Briggs, J. A. G., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3801 · Cited by 293
Engineering of soluble bacteriorhodopsin
Nikolaev, A., Orlov, Y., Tsybrov, F., Kuznetsova, E., Shishkin, P., Kuzmin, A., Mikhailov, A., Nikolaeva, Y. S., Anuchina, A., Chizhov, I., et al. (2025) · Chemical Science · doi:10.1039/d5sc02453f · Cited by 6
Metadata
- Authors
- Schafmeister, C. E., Miercke, L. J. W., & Stroud, R. M.
- Venue
- Science
- Published
- 1993-10-29
- Volume
- 262
- Issue
- 5134
- Pages
- 734-738
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2079148256
- Cited by
- 201
- References
- 1
- FWCI
- 7.24
- 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: Structure at 2.5 Å of a Designed Peptide that Maintains Solubility of Membrane Proteins. https://app.cochat.ai/papers/10.1126/science.8235592
- The paper
- Schafmeister, C. E., Miercke, L. J. W., & Stroud, R. M. (1993). Structure at 2.5 Å of a Designed Peptide that Maintains Solubility of Membrane Proteins. Science. https://doi.org/10.1126/science.8235592
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.