Unknown

Dataset Information

0

The Hydrophobic Effect in Solute Partitioning and Interfacial Tension.


ABSTRACT: Studies of the partitioning of hydrophobic solutes between water and nonpolar solvents provide estimates for the energy cost of creating hydrophobic-water contacts. This energy is a factor of three lower than the work of adhesion derived from interfacial tension measurements. This discrepancy noted by Tanford in 1979 is widely viewed as a serious challenge to our understanding of hydrophobic interactions. However, the interfacial energy of a water-alkane interface depends on chain length. A simple analysis of published data shows that the loss of rotational freedom of an alkane chain at an interface accounts quantitatively for the length-dependent contribution to interfacial tension, leaving a length-independent contribution very close to the free energy of transfer per unit of solvent accessible surface area. This analysis thus clarifies the discrepancy between the thermodynamic and interfacial tension measurements of hydrophobic interaction energy. Alkanes do not loose rotational freedom when transferred between two different liquid phases but they do at an interface. This reconciles the difference between microscopic and macroscopic measurements. Like the partitioning free energy, the work of adhesion also has a large entropy and small enthalpy at 20 (o)C.

SUBMITTER: Jackson MB 

PROVIDER: S-EPMC4728684 | biostudies-other | 2016 Jan

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC9911786 | biostudies-literature
| S-EPMC7364585 | biostudies-literature
| S-EPMC5537356 | biostudies-literature
| S-EPMC8591605 | biostudies-literature
| S-EPMC5458086 | biostudies-literature
| S-EPMC4975753 | biostudies-other
| S-EPMC3694758 | biostudies-literature
| S-EPMC9148048 | biostudies-literature
| S-EPMC5522447 | biostudies-literature
| S-EPMC3511739 | biostudies-literature