Skip to main content

Some NLM-NCBI services and products are experiencing heavy traffic, which may affect performance and availability. We apologize for the inconvenience and appreciate your patience. For assistance, please contact our Help Desk at info@ncbi.nlm.nih.gov.

Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 Oct;74(10):4144–4145. doi: 10.1073/pnas.74.10.4144

Use of solvent cavity area and number of packed solvent molecules around a solute in regard to hydrocarbon solubilities and hydrophobic interactions

Robert B Hermann 1
PMCID: PMC431892  PMID: 16592439

Abstract

Two currently used methods of calculating the area of contact between a solute molecule and the solvent are examined and some important differences are pointed out. Some pitfalls and uncertainties in the application of the concept of molecular surface area to the quantitative estimation of unitary free energies of solution are discussed.

Keywords: molecular surface area

Full text

PDF
4144

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Amidon G. L., Yalkowsky S. H., Leung S. Solubility of nonelectrolytes in polar solvents II: solubility of aliphatic alcohols in water. J Pharm Sci. 1974 Dec;63(12):1858–1866. doi: 10.1002/jps.2600631207. [DOI] [PubMed] [Google Scholar]
  2. Chothia C. Hydrophobic bonding and accessible surface area in proteins. Nature. 1974 Mar 22;248(446):338–339. doi: 10.1038/248338a0. [DOI] [PubMed] [Google Scholar]
  3. Chothia C., Janin J. Principles of protein-protein recognition. Nature. 1975 Aug 28;256(5520):705–708. doi: 10.1038/256705a0. [DOI] [PubMed] [Google Scholar]
  4. Chothia C. Structural invariants in protein folding. Nature. 1975 Mar 27;254(5498):304–308. doi: 10.1038/254304a0. [DOI] [PubMed] [Google Scholar]
  5. Hermann R. E. Selective, conservative operations for cancer of the breast. Cleve Clin Q. 1975 Summer;42(2):163–169. doi: 10.3949/ccjm.42.2.163. [DOI] [PubMed] [Google Scholar]
  6. Lee B., Richards F. M. The interpretation of protein structures: estimation of static accessibility. J Mol Biol. 1971 Feb 14;55(3):379–400. doi: 10.1016/0022-2836(71)90324-x. [DOI] [PubMed] [Google Scholar]
  7. Reynolds J. A., Gilbert D. B., Tanford C. Empirical correlation between hydrophobic free energy and aqueous cavity surface area. Proc Natl Acad Sci U S A. 1974 Aug;71(8):2925–2927. doi: 10.1073/pnas.71.8.2925. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Shrake A., Rupley J. A. Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J Mol Biol. 1973 Sep 15;79(2):351–371. doi: 10.1016/0022-2836(73)90011-9. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES