The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
A de novo peptide hexamer with a mutable channel
Open accessAbstract
The design of new proteins that expand the repertoire of natural protein structures represents a formidable challenge. Success in this area would increase understanding of protein structure, and present new scaffolds that could be exploited in biotechnology and synthetic biology. Here we describe the design, characterisation and X-ray crystal structure of a new coiled-coil protein. The de novo sequence forms a stand-alone, parallel, 6-helix bundle with a channel running through it. Although lined exclusively by hydrophobic leucine and isoleucine side chains, the 6 Å channel is permeable to water. One layer of leucine residues within the channel is mutable accepting polar aspartic acid (Asp) and histidine (His) side chains, and leading to subdivision and organization of solvent within the lumen. Moreover, these mutants can be combined to form a stable and unique (Asp-His)3 heterohexamer. These new structures provide a basis for engineering de novo proteins with new functions.
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
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490
The Design of Coiled-Coil Structures and Assemblies
Woolfson, D. N. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70004-8 · Cited by 585
Self-citationWalshaw, J., & Woolfson, D. N. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4545 · Cited by 357
Self-citationParry, D. A. D., Fraser, R. D. B., & Squire, J. M. (2008) · Journal of Structural Biology · doi:10.1016/j.jsb.2008.01.016 · Cited by 264
Predicting oligomerization states of coiled coils
Woolfson, D. N., & Alber, T. (1995) · Protein Science · doi:10.1002/pro.5560040818 · Cited by 214
Self-citationExtended knobs-into-holes packing in classical and complex coiled-coil assemblies☆
Walshaw, J., & Woolfson, D. N. (2003) · Journal of Structural Biology · doi:10.1016/j.jsb.2003.10.014 · Cited by 104
Self-citationSCORER 2.0: an algorithm for distinguishing parallel dimeric and trimeric coiled-coil sequences
Armstrong, C. T., Vincent, T. L., Green, P. J., & Woolfson, D. N. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr299 · Cited by 49
Self-citation
Cited by
The coming of age of de novo protein design
Huang, P.-S., Boyken, S. E., & Baker, D. (2016) · Nature · doi:10.1038/nature19946 · Cited by 1,478
The molecular architecture of lamins in somatic cells
Turgay, Y., Eibauer, M., Goldman, A. E., Shimi, T., Khayat, M., Ben-Harush, K., Dubrovsky-Gaupp, A., Sapra, K. T., Goldman, R. D., & Medalia, O. (2017) · Nature · doi:10.1038/nature21382 · Cited by 423
Deng, C., Wu, J., Cheng, R., Meng, F., Klok, H.-A., & Zhong, Z. (2014) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2013.10.008 · Cited by 371
Computational design of water-soluble α-helical barrels
Thomson, A. R., Wood, C. W., Burton, A. J., Bartlett, G. J., Sessions, R. B., Brady, R. L., & Woolfson, D. N. (2014) · Science · doi:10.1126/science.1257452 · Cited by 330
Self-citationSmart Self‐Assembled Hybrid Hydrogel Biomaterials
Kopeček, J., & Yang, J. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201201040 · Cited by 313
Metadata
- Authors
- Zaccai, N. R., Chi, B., Thomson, A. R., Boyle, A. L., Bartlett, G. J., Bruning, M., Linden, N., Sessions, R. B., Booth, P. J., Brady, R. L., & Woolfson, D. N.
- Venue
- Nature Chemical Biology
- Published
- 2011-10-30
- Volume
- 7
- Issue
- 12
- Pages
- 935-941
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2148306017
- Cited by
- 192
- References
- 9
- FWCI
- 6.35
- 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: A de novo peptide hexamer with a mutable channel. https://app.cochat.ai/papers/10.1038/nchembio.692
- The paper
- Zaccai, N. R., Chi, B., Thomson, A. R., Boyle, A. L., Bartlett, G. J., Bruning, M., Linden, N., Sessions, R. B., Booth, P. J., Brady, R. L., & Woolfson, D. N. (2011). A de novo peptide hexamer with a mutable channel. Nature Chemical Biology. https://doi.org/10.1038/nchembio.692
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.
