The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Impact of Protein Denaturants and Stabilizers on Water Structure
Abstract
It is of great interest to determine how solutes such as urea, sugars, guanidinium salts, and trimethylamine N-oxide affect the stability, solubility, and solvation of globular proteins. A key hypothesis in this field states that solutes affect protein stability indirectly by making or breaking water structure. We used a new technique, pressure perturbation calorimetry, to measure the temperature dependence of a solute's partial compressibility. Using fundamental thermodynamic relations, we converted these data to the pressure dependence of the partial heat capacity to examine the impact of protein stabilizing and denaturing solutes on water structure by applying the classic two-state mixture model for water. Contrary to widely held expectations, we found no correlation between a solute's impact on water structure and its effect on protein stability. Our results indicate that efforts to explain solute effects should focus on other hypotheses, including those based on preferential interaction and excluded volume.
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Cited by
Interactions between macromolecules and ions: the Hofmeister series
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A molecular mechanism for osmolyte-induced protein stability
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Metadata
- Authors
- Batchelor, J. D., Olteanu, A., Tripathy, A., & Pielak, G. J.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2004-01-23
- Volume
- 126
- Issue
- 7
- Pages
- 1958-1961
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1978188750
- Cited by
- 324
- References
- 16
- FWCI
- 21.13
- Type
- journal article
- Language
- en
- Open access
- closed
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