Show simple item record  

dc.contributor.authorFinney, John L.
dc.contributor.authorBowron, D.T.
dc.contributor.authorDaniel, Roy M.
dc.contributor.authorTimmins, P.A.
dc.contributor.authorRoberts, Mark A.
dc.identifier.citationFinney, J.L., Bowron, D.T., Daniel, R.M., Timmins, P.A. & Roberts, M.A. (2003). Molecular and mesoscale structures in hydrophobically driven aqueous solutions. Biophysical Chemistry, 105(2-3), Biophysical Chemisty, 105(2-3), 391-409.en_NZ
dc.description.abstractSince Kauzmann's seminal 1959 paper, the hydrophobic interaction has dominated thinking on the forces that control protein folding and stability. Despite its wide importance in chemistry and biology, our understanding of this interaction at the molecular level remains poor, with little experimental evidence to support the idea of water ordering close to a non-polar group that is at the centre of the standard model for the source of the entropic driving force. Developments over recent years in neutron techniques now enable us to see directly how a non-polar group actually affects the molecular structure of the water in its immediate neighbourhood. On the basis of such work on aqueous solutions of small alcohols, the generally accepted standard model is found to be wanting, and alternative sources of the entropic driving force are suggested. Moreover, the fact that we can now follow changes in hydrogen bonding as the alcohol concentration is varied gives us the possibility of explaining the concentration dependence of the enthalpy of mixing. Complementary studies of solute association on the mesoscopic scale show a rich concentration and temperature behaviour, which reflects a complex balance of polar and non-polar interactions. Unravelling the detailed nature of this balance in simple aqueous amphiphiles may lead to a better understanding of the forces that control biomolecular structural stability and interactions.en_NZ
dc.subjectnon-polar interactionsen_NZ
dc.subjectaqueous solution structureen_NZ
dc.subjectentropic driving forceen_NZ
dc.subjectsolution structureen_NZ
dc.subjectprotein stabilityen_NZ
dc.subjecthydrophobic interactionen_NZ
dc.titleMolecular and mesoscale structures in hydrophobically driven aqueous solutionsen_NZ
dc.typeJournal Articleen_NZ
dc.relation.isPartOfBiophysical Chemistryen_NZ

Files in this item


There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record