Issue 0, 1975

Reassessment of hydrophobic bonding

Abstract

Hydrophobic bonding theory is re-examined in the light of 13C relaxation time (T1) measurements, which indicate that water is unique in its ability to restrict the motion of hydrophobic parts of solute molecules. The motional restriction is shown to account for most of the entropy change on solution that has hitherto been ascribed to “structure making.” A simple theory of the restriction mechanism is advanced which also explains the observed enthalpies of solution and the isotope effects.

Article information

Article type
Paper

J. Chem. Soc., Faraday Trans. 1, 1975,71, 2303-2309

Reassessment of hydrophobic bonding

O. W. Howarth, J. Chem. Soc., Faraday Trans. 1, 1975, 71, 2303 DOI: 10.1039/F19757102303

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements