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Title: | Enthalpy of Interaction between some Globular Proteins and Sodium n-Dodecyl Sulphate in Aqueous Solution |
Authors: | Tipping, Edward Jones, Malcolm N. Skinner, Henry A. |
Keywords: | Chemistry Enthalpy of Interaction Globular Proteins Journal of the Chemical Society : Faraday Transaction - I |
Issue Date: | 1974 |
Publisher: | Journal of the Chemical Society : Faraday Transaction - I. The Chemical Society, London. 1974, 70 (07) |
Abstract: | 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. |
URI: | http://dspace.bits-pilani.ac.in:8080/jspui/handle/123456789/19006 |
Appears in Collections: | Journal Articles (before-1995) |
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