Statistical Effects of the Binding of Ionic Surfactant to Protein

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 mode...

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Veröffentlicht in:Journal of colloid and interface science 1997-08, Vol.192 (2), p.415-419
Hauptverfasser: Bordbar, A.K., Saboury, A.A., Housaindokht, M.R., Moosavi-Movahedi, A.A.
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container_issue 2
container_start_page 415
container_title Journal of colloid and interface science
container_volume 192
creator Bordbar, A.K.
Saboury, A.A.
Housaindokht, M.R.
Moosavi-Movahedi, A.A.
description 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 sodiumn-dodecyl sulfate binding to ribonuclease A and lysozyme.
doi_str_mv 10.1006/jcis.1997.4999
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source Elsevier ScienceDirect Journals
subjects binding model
Chemistry
Exact sciences and technology
General and physical chemistry
Gibbs free energy
ionic surfactant
protein
Surface physical chemistry
Surface-active agents: properties
title Statistical Effects of the Binding of Ionic Surfactant to Protein
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