The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Amino Acid Preferences for Specific Locations at the Ends of α Helices
Abstract
A definition based on α-carbon positions and a sample of 215 α helices from 45 different globular protein structures were used to tabulate amino acid preferences for 16 individual positions relative to the helix ends. The interface residue, which is half in and half out of the helix, is called the N-cap or C-cap, whichever is appropriate. The results confirm earlier observations, such as asymmetrical charge distributions in the first and last helical turn, but several new, sharp preferences are found as well. The most striking of these are a 3.5:1 preference for Asn at the N-cap position, and a preference of 2.6:1 for Pro at N-cap + 1. The C-cap position is overwhelmingly dominated by Gly, which ends 34 percent of the helices. Hydrophobic residues peak at positions N-cap + 4 and C-cap - 4.
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
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a001 · Cited by 2,172
Cited by
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648
ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs
Ye, J., Rawson, R. B., Komuro, R., Chen, X., Davé, U. P., Prywes, R., Brown, M. S., & Goldstein, J. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00133-7 · Cited by 1,871
Influence of proline residues on protein conformation
MacArthur, M. W., & Thornton, J. M. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90721-h · Cited by 1,189
The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation
Davis, R. L., Cheng, P.-F., Lassar, A. B., & Weintraub, H. (1990) · Cell · doi:10.1016/0092-8674(90)90088-v · Cited by 765
Elucidating the folding problem of helical peptides using empirical parameters
Muñoz, V., & Serrano, L. (1994) · Nature Structural & Molecular Biology · doi:10.1038/nsb0694-399 · Cited by 721
Prendergast, G. C., Lawe, D., & Ziff, E. B. (1991) · Cell · doi:10.1016/0092-8674(91)90457-a · Cited by 558
Collawn, J. F., Stangel, M., Kuhn, L. A., Esekogwu, V., Jing, S., Trowbridge, I. S., & Tainer, J. A. (1990) · Cell · doi:10.1016/0092-8674(90)90509-d · Cited by 518
Stabilization of alpha-helical structures in short peptides via end capping
Forood, B., Feliciano, E. J., & Nambiar, K. P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.3.838 · Cited by 235
Friedman, A. D., & McKnight, S. L. (1990) · Genes & Development · doi:10.1101/gad.4.8.1416 · Cited by 162
The Role of Proline and Glycine in Determining the Backbone Flexibility of a Channel-Forming Peptide
Jacob, J., Duclohier, H., & Cafiso, D. S. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77298-x · Cited by 139
An artificial PPR scaffold for programmable RNA recognition
Coquille, S., Filipovska, A., Chia, T., Rajappa, L., Lingford, J. P., Razif, M. F. M., Thore, S., & Rackham, O. (2014) · Nature Communications · doi:10.1038/ncomms6729 · Cited by 120
Blaber, M., Lindstrom, J. D., Gassner, N., Xu, J., Heinz, D. W., & Matthews, B. W. (1993) · Biochemistry · doi:10.1021/bi00093a013 · Cited by 93
Identification of a Novel Domain in the Aryl Hydrocarbon Receptor Required for DNA Binding
Fukunaga, B. N., & Hankinson, O. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.7.3743 · Cited by 91
Hariharan, V., & Hancock, W. O. (2009) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-009-0059-5 · Cited by 82
Schuermann, M., Hunter, J. B., Hennig, G., & Müller, R. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.4.739 · Cited by 80
Urbanek, A., Popovic, M., Morató, A., Estaña, A., Elena-Real, C. A., Mier, P., Fournet, A., Allemand, F., Delbecq, S., Andrade-Navarro, M. A., et al. (2020) · Structure · doi:10.1016/j.str.2020.04.008 · Cited by 66
AAontology: An Ontology of Amino Acid Scales for Interpretable Machine Learning
Breimann, S., Kamp, F., Steiner, H., & Frishman, D. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168717 · Cited by 15
Onwunma, J., Binsabaan, S., Allen, S. P., Thanthirige, S. R., Gaur, D., Sankaran, B., & Wohlever, M. L. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00745-9 · Cited by 10
Tetramerisation governs SALL transcription factor function in development and disease
Giuliani, S., Chhatbar, K., Wear, M., Guy, J., Mathieson, T., Burdett, H., George, L., Alston, G., Spanos, C., McHugh, T., et al. (2025) · bioRxiv · doi:10.1101/2025.10.27.684836
Metadata
- Authors
- Richardson, J. S., & Richardson, D. C.
- Venue
- Science
- Published
- 1988-06-17
- Volume
- 240
- Issue
- 4859
- Pages
- 1648-1652
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2081359387
- Cited by
- 1,364
- References
- 2
- FWCI
- 18.42
- 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
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.
