| Literature DB >> 9367564 |
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Abstract
Two different theories based on a multiple equilibrium model for analysing the binding data for ionic surfactant-protein interactions are investigated and modified, and intrinsic and statistical Gibbs free energies of binding per mole of surfactant are estimated. The characterization of the two models and interpretation of the binding process in terms of intrinsic and statistical binding free energies are discussed. These theories are applied to analysis of sodium n-dodecyl sulfate binding to ribonuclease A and lysozyme. Copyright 1997Academic PressEntities:
Year: 1997 PMID: 9367564 DOI: 10.1006/jcis.1997.4999
Source DB: PubMed Journal: J Colloid Interface Sci ISSN: 0021-9797 Impact factor: 8.128