The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
A role for surface hydrophobicity in protein‐protein recognition
Open accessAbstract
The role of hydrophobicity as a determinant of protein‐protein interactions is examined. Surfaces of apo‐protein targets comprising 9 classes of enzymes, 7 antibody fragments, hirudin, growth hormone, and retinol‐binding protein, and their associated ligands with available X‐ray structures for their complexed forms, are scanned to determine clusters of surface‐accessible amino acids. Clusters of surface residues are ranked on the basis of the hydrophobicity of their constituent amino acids. The results indicate that the location of the co‐crystallized ligand is commonly found to correspond with one of the strongest hydrophobic clusters on the surface of the target molecule. In 25 of 38 cases, the correspondence is exact, with the position of the most hydrophobic cluster coinciding with more than one‐third of the surface buried by the bound ligand. The remaining 13 cases demonstrate this correspondence within the top 6 hydrophobic clusters. These results suggest that surface hydrophobicity can be used to identify regions of a protein's surface most likely to interact with a binding ligand. This fast and simple procedure may be useful for identifying small sets of well‐defined loci for possible ligand attachment.
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
Density-functional thermochemistry. III. The role of exact exchange
Becke, A. D. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464913 · Cited by 103,767
The protein data bank: A computer-based archival file for macromolecular structures
Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., & Tasumi, M. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80200-3 · Cited by 8,578
Nicholls, A., Sharp, K. A., & Honig, B. (1991) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,240
Some Factors in the Interpretation of Protein Denaturation
Kauzmann, W. (1959) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60608-7 · Cited by 4,870
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,800
Solvent-Accessible Surfaces of Proteins and Nucleic Acids
Connolly, M. L. (1983) · Science · doi:10.1126/science.6879170 · Cited by 2,745
Walker, C. H. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80071-3 · Cited by 2,696
Goodford, P. J. (1985) · Journal of Medicinal Chemistry · doi:10.1021/jm00145a002 · Cited by 2,634
Analytical molecular surface calculation
Connolly, M. L. (1983) · Journal of Applied Crystallography · doi:10.1107/s0021889883010985 · Cited by 2,508
A geometric approach to macromolecule-ligand interactions
Kuntz, I. D., Blaney, J. M., Oatley, S. J., Langridge, R., & Ferrin, T. E. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90153-x · Cited by 2,278
Cited by
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684
Principles of docking: An overview of search algorithms and a guide to scoring functions
Halperin, I., Ma, B., Wolfson, H., & Nussinov, R. (2002) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10115 · Cited by 1,294
Hot spots—A review of the protein–protein interface determinant amino‐acid residues
Moreira, I. S., Fernandes, P. A., & Ramos, M. J. (2007) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.21396 · Cited by 760
Ranganathan, R., Lu, K. P., Hunter, T., & Noel, J. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80273-1 · Cited by 699
Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?
Keskin, O., Gursoy, A., Ma, B., & Nussinov, R. (2008) · Chemical Reviews · doi:10.1021/cr040409x · Cited by 697
Metadata
- Authors
- Young, L., Jernigan, R. L., & Covell, D. G.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 1994-05
- Volume
- 3
- Issue
- 5
- Pages
- 717-729
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2101362041
- Cited by
- 391
- References
- 46
- FWCI
- 4.29
- Type
- journal article
- Language
- en
- Open access
- bronze
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 role for surface hydrophobicity in protein‐protein recognition. https://app.cochat.ai/papers/10.1002/pro.5560030501
- The paper
- Young, L., Jernigan, R. L., & Covell, D. G. (1994). A role for surface hydrophobicity in protein‐protein recognition. Protein Science. https://doi.org/10.1002/pro.5560030501
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.
