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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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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