Browsing by Author "Tipping, Edward"

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    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.