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Binding Behaviour and Conformational Properties of Globular Proteins in the Presence of Immobilised Non-polar Ligands Used in Reversed-phase Liquid Chromatography by Reinhard I. Boysen; Agnes J.O. Jong; Milton T.W. Hearn is a Chemistry article available to read on EtoBox.

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The thermodynamic and extra-thermodynamic dependencies of five types of cytochrome c in water-acetonitrile mixtures of different composition in the presence of immobilised n-octyl ligands as a function of temperature from 278 K to 338 K have been investigated. The corresponding enthalpic, entropic and heat capacity parameters, deltaHdegrees assoc, deltaS degrees assoc and delta C degrees p, have been evaluated from the observed non-linear Van't Hoff plots of these globular proteins in these heterogeneous systems. The relationships between the free energy dependencies, various molecular parameters and extra-thermodynamic dependencies (empirical correlations) of these protein-non-polar ligand interactions have also been examined. Thus, the involvement of enthalpy-entropy compensation effects has been documented for the binding of these cytochrome cs to solvated n-octyl ligands. Moreover, the results confirm that this experimental approach permits changes in molecular surface area due to the unfolding of these proteins on association with non-polar ligands as a function of temperature to be correlated with other biophysical properties. This study thus provides a general procedure wher

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Author

Reinhard I. Boysen; Agnes J.O. Jong; Milton T.W. Hearn

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1873-3778)

Published

2005

Language

EN

Field

Chemistry (Physical Sciences)