The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Crystal Structure of a Ten-Amino Acid Protein
Open accessAbstract
What is the smallest protein? This is actually not such a simple question to answer, because there is no established consensus among scientists as to the definition of a protein. We describe here a designed molecule consisting of only 10 amino acids. Despite its small size, its essential characteristics, revealed by its crystal structure, solution structure, thermal stability, free energy surface, and folding pathway network, are consistent with the properties of natural proteins. The existence of this kind of molecule deepens our understanding of proteins and impels us to define an "ideal protein" without inquiring whether the molecule actually occurs in nature.
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
Toward an outline of the topography of a realistic protein-folding funnel.
Onuchic, J. N., Wolynes, P. G., Luthey-Schulten, Z., & Socci, N. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.8.3626 · Cited by 523
Cited by
How fast-folding proteins fold
Lindorff-Larsen, K., Piana, S., Dror, R. O., & Shaw, D. E. (2011) · Science · doi:10.1126/science.1208351 · Cited by 1,980
Quantum Chemistry on Graphical Processing Units. 2. Direct Self-Consistent-Field Implementation
Ufimtsev, I. S., & Martinez, T. J. (2009) · Journal of Chemical Theory and Computation · doi:10.1021/ct800526s · Cited by 451
TorchMD: A Deep Learning Framework for Molecular Simulations
Doerr, S., Majewski, M., Pérez, A., Krämer, A., Clementi, C., Noe, F., Giorgino, T., & De Fabritiis, G. (2021) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.0c01343 · Cited by 230
“Finally, we present a coarse-grained simulation of a miniprotein, chigno-lin, 36 using NNP trained on all-atom MD simulation data.”
MethodGreener, J. G., & Jones, D. T. (2021) · PLOS ONE · doi:10.1371/journal.pone.0256990 · Cited by 29
Metadata
- Authors
- Honda, S., Akiba, T., Kato, Y. S., Sawada, Y., Sekijima, M., Ishimura, M., Ooishi, A., Watanabe, H., Odahara, T., & Harata, K.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-10-25
- Volume
- 130
- Issue
- 46
- Pages
- 15327-15331
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1968707111
- Cited by
- 188
- References
- 1
- FWCI
- 2.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
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: Crystal Structure of a Ten-Amino Acid Protein. https://app.cochat.ai/papers/10.1021/ja8030533
- The paper
- Honda, S., Akiba, T., Kato, Y. S., Sawada, Y., Sekijima, M., Ishimura, M., Ooishi, A., Watanabe, H., Odahara, T., & Harata, K. (2008). Crystal Structure of a Ten-Amino Acid Protein. Journal of the American Chemical Society. https://doi.org/10.1021/ja8030533
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.