Title : A direct calorimetric determination of denaturation enthalpy for lysozyme in sodium dodecyl sulfate.

Pub. Date : 2008 Feb 15

PMID : 17889513






6 Functional Relationships(s)
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1 A direct calorimetric determination of denaturation enthalpy for lysozyme in sodium dodecyl sulfate. Sodium Dodecyl Sulfate lysozyme Homo sapiens
2 Thermodynamics of the interaction between sodium dodecyl sulfate (SDS) with lysozyme were investigated at pH 7.0 and 27 degrees C in phosphate buffer by isothermal titration calorimetry. Sodium Dodecyl Sulfate lysozyme Homo sapiens
3 Thermodynamics of the interaction between sodium dodecyl sulfate (SDS) with lysozyme were investigated at pH 7.0 and 27 degrees C in phosphate buffer by isothermal titration calorimetry. Sodium Dodecyl Sulfate lysozyme Homo sapiens
4 The new solvation model was used to reproduce the enthalpies of lysozyme-SDS interaction over the whole range of SDS concentrations. Sodium Dodecyl Sulfate lysozyme Homo sapiens
5 The new solvation model was used to reproduce the enthalpies of lysozyme-SDS interaction over the whole range of SDS concentrations. Sodium Dodecyl Sulfate lysozyme Homo sapiens
6 At low concentrations of SDS, the binding is mainly electrostatic, with some simultaneous interaction of the hydrophobic tail with nearby hydrophobic patches on the lysozyme. Sodium Dodecyl Sulfate lysozyme Homo sapiens