Statistical Effects of the Binding of Ionic Surfactant to Protein
โ Scribed by A.K. Bordbar; A.A. Saboury; M.R. Housaindokht; A.A. Moosavi-Movahedi
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 135 KB
- Volume
- 192
- Category
- Article
- ISSN
- 0021-9797
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โฆ Synopsis
THEORY Two different theories based on a multiple equilibrium model for analysing the binding data for ionic surfactant-protein interac-
The binding of ligand, S, to a protein, P, can be described tions are investigated and modified, and intrinsic and statistical by a series of equilibria. These multiple equilibria can be Gibbs free energies of binding per mole of surfactant are estimated. shown in terms of stoichiometric binding constants which The characterization of the two models and interpretation of the do not distinguish between species that have the same numbinding process in terms of intrinsic and statistical binding free ber of bound ligands; i.e., the species PS j can be formed in energies are discussed. These theories are applied to analysis of several ways, depending on which particular set of j sites sodium n-dodecyl sulfate binding to ribonuclease A and lysozyme. are occupied. For binding of ionic surfactant to water-soluble
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