Research Commons
      • Browse 
        • Communities & Collections
        • Titles
        • Authors
        • By Issue Date
        • Subjects
        • Types
        • Series
      • Help 
        • About
        • Collection Policy
        • OA Mandate Guidelines
        • Guidelines FAQ
        • Contact Us
      • My Account 
        • Sign In
        • Register
      View Item 
      •   Research Commons
      • University of Waikato Research
      • Science and Engineering
      • Science and Engineering Papers
      • View Item
      •   Research Commons
      • University of Waikato Research
      • Science and Engineering
      • Science and Engineering Papers
      • View Item
      JavaScript is disabled for your browser. Some features of this site may not work without it.

      Molecular and mesoscale structures in hydrophobically driven aqueous solutions

      Finney, John L.; Bowron, D.T.; Daniel, Roy M.; Timmins, P.A.; Roberts, Mark A.
      DOI
       10.1016/S0301-4622(03)00104-2
      Find in your library  
      Citation
      Export citation
      Finney, 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.
      Permanent Research Commons link: https://hdl.handle.net/10289/4448
      Abstract
      Since 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.
      Date
      2003-09
      Type
      Journal Article
      Publisher
      Elsevier
      Collections
      • Science and Engineering Papers [3121]
      Show full item record  

      Usage

       
       
       

      Usage Statistics

      For this itemFor all of Research Commons

      The University of Waikato - Te Whare Wānanga o WaikatoFeedback and RequestsCopyright and Legal Statement