The DOI matches its Crossref record; 104 of the 104 references it cites were found in a registry or an index.
A View of the Hydrophobic Effect
Abstract
Oil and water do not mix. The disaffinity of oil for water, with its unusual temperature dependence, is called the hydrophobic effect. It is important to understand the factors underlying the hydrophobic effect because they appear to play key roles in membrane and micelle formation, protein folding, ligand-protein and protein−protein binding, chromatographic retention, possibly nucleic acid interactions, and the partitioning of drugs, metabolites, and toxins throughout the environment and living systems. Here, we survey experimental and theoretical studies of nonpolar solute partitioning into water. We note that the hydrophobic effect is not just due to “water ordering” and not merely due to small size effects of water. The properties vary substantially with temperature and solute shape. Also, we discuss the limitations of using oil/water partitioning as the basis for some thermodynamic models in chemistry and biology.
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Metadata
- Authors
- Southall, N. T., Dill, K. A., & Haymet, A. D. J.
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 2001-12-20
- Volume
- 106
- Issue
- 3
- Pages
- 521-533
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- OpenAlex
- W1984903816
- Cited by
- 913
- References
- 104
- FWCI
- 21.57
- 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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
