Journal Articles (before-1995)

Permanent URI for this collectionhttp://localhost:4000/handle/123456789/16938

Browse

Author: search.filters.author.Skinner, Henry A.Subject: search.filters.subject.Globular Proteins

Search Results

Now showing 1 - 1 of 1
  • No Thumbnail Available
    Item
    Enthalpy of Interaction between some Globular Proteins and Sodium n-Dodecyl Sulphate in Aqueous Solution
    (Journal of the Chemical Society : Faraday Transaction - I. The Chemical Society, London. 1974, 70 (07), 1974) Tipping, Edward; Jones, Malcolm N.; Skinner, Henry A.
    The enthalpy of binding of sodium n-dodecyl sulphate (SDS) to scrum albumin, ovalbumin and ribonuclease A has been measured by microcalorimetry over the temperature range 18.5 to 32.0 C. The amount of SDS bound to the proteins has been measured over a wide range of SDS concentration by equilibrium dialysis. Changes in protein conformation have been monitored by viscometry. The results are consistent with a mechanism in which SDS binds initially to ionic sites on the protein molecules and initiates chain unfolding. At high binding levels the interaction is predominantly of a hydrophobic nature.