Binding Data Analysis for Interaction of n- Alkyl Sulfates with Insulin
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Abstract:
The binding data for interaction of a homologous series of n-alkyl sulfates with alkyl chainlengths from C8 to C12 with insulin were analyzed on basis of Hill equation for two classes ofbinding sites .The intrinsic Gibbs free energies were calculated and resolute on basis ofelectrostatic and hydrophobic contributions The estimation of these contributions reveals themajor role of electrostatic interactions on first binding set and the minor one in the second.
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binding data analysis for interaction of n- alkyl sulfates with insulin
the binding data for interaction of a homologous series of n-alkyl sulfates with alkyl chainlengths from c8 to c12 with insulin were analyzed on basis of hill equation for two classes ofbinding sites .the intrinsic gibbs free energies were calculated and resolute on basis ofelectrostatic and hydrophobic contributions the estimation of these contributions reveals themajor role of electrostatic i...
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Journal title
volume 1 issue 2
pages 25- 28
publication date 2004-08-01
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