A Computational Study of Cation−π Interactions vs Salt Bridges in Aqueous Media: Implications for Protein Engineering
- Creators
- Gallivan, Justin P.
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Dougherty, Dennis A.
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.
Additional Information
© 2000 American Chemical Society. Received May 27, 1999. Revised Manuscript Received December 1, 1999. Publication Date (Web): January 21, 2000. We gratefully acknowledge Dr. Jiabo Li, Professor Christopher Cramer, and Professor Donald Truhlar of the University of Minnesota for providing the Gaussian Solvation Module and for many helpful discussions. J.P.G. acknowledges the Eastman Kodak Corporation for generous fellowship support. This work was supported by the NIH (NS 34407).Attached Files
Published - ja991755c.pdf
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Additional details
- Eprint ID
- 77334
- Resolver ID
- CaltechAUTHORS:20170510-091933346
- NS 34407
- NIH
- Eastman Kodak Company
- Created
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2017-05-16Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field