The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
A Computational Study of Cation−π Interactions vs Salt Bridges in Aqueous Media: Implications for Protein Engineering
Abstract
A direct comparison of the energetic significance of a representative salt bridge vs a representative cation−π interaction in aqueous media and in a range of organic solvents is presented using ab initio electronic structures and the SM5.42R/HF solvation model of Cramer and Truhlar. The cation−π interaction shows a well depth of 5.5 kcal/mol in water, significantly larger than the 2.2 kcal/mol seen for the salt bridge. Consistent with this idea, a survey of the Protein Data Bank reveals that energetically significant cation−π interactions are rarely completely buried within proteins, but prefer to be exposed to solvent. These results suggest that engineering surface-exposed cation−π interactions could be a novel way to enhance protein stability.
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Cites
Semianalytical treatment of solvation for molecular mechanics and dynamics
Still, W. C., Tempczyk, A., Hawley, R. C., & Hendrickson, T. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00172a038 · Cited by 3,643
Classical Electrostatics in Biology and Chemistry
Honig, B., & Nicholls, A. (1995) · Science · doi:10.1126/science.7761829 · Cited by 2,879
Cation-π Interactions in Chemistry and Biology: A New View of Benzene, Phe, Tyr, and Trp
Dougherty, D. A. (1996) · Science · doi:10.1126/science.271.5246.163 · Cited by 2,656
Self-citationImplicit Solvation Models: Equilibria, Structure, Spectra, and Dynamics
Cramer, C. J., & Truhlar, D. G. (1999) · Chemical Reviews · doi:10.1021/cr960149m · Cited by 2,308
Cation-π interactions in structural biology
Gallivan, J. P., & Dougherty, D. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.17.9459 · Cited by 1,997
Self-citationDe Novo Protein Design: Fully Automated Sequence Selection
Dahiyat, B. I., & Mayo, S. L. (1997) · Science · doi:10.1126/science.278.5335.82 · Cited by 1,145
Conservation and prediction of solvent accessibility in protein families
Rost, B., & Sander, C. (1994) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340200303 · Cited by 665
Do salt bridges stabilize proteins? A continuum electrostatic analysis
Hendsch, Z. S., & Tidor, B. (1994) · Protein Science · doi:10.1002/pro.5560030206 · Cited by 637
Kumpf, R. A., & Dougherty, D. A. (1993) · Science · doi:10.1126/science.8378771 · Cited by 636
Self-citationTransient folding intermediates characterized by protein engineering
Matouschek, A., Kellis, J. T., Serrano, L., Bycroft, M., & Fersht, A. R. (1990) · Nature · doi:10.1038/346440a0 · Cited by 451
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COLLINS, K. (2004) · Methods · doi:10.1016/j.ymeth.2004.03.021 · Cited by 1,091
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Hofman, A. H., van Hees, I. A., Yang, J., & Kamperman, M. (2018) · Advanced Materials · doi:10.1002/adma.201704640 · Cited by 652
Recent approaches in designing bioadhesive materials inspired by mussel adhesive protein
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Cui, C., & Liu, W. (2021) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2021.101388 · Cited by 557
Price, A. J., Jacques, D. A., McEwan, W. A., Fletcher, A. J., Essig, S., Chin, J. W., Halambage, U. D., Aiken, C., & James, L. C. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004459 · Cited by 284
Metadata
- Authors
- Gallivan, J. P., & Dougherty, D. A.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2000-01-21
- Volume
- 122
- Issue
- 5
- Pages
- 870-874
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2067592712
- Cited by
- 448
- References
- 15
- FWCI
- 13.76
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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