Binding behaviour and conformational properties of globular proteins in the presence of immobilised non-polar ligands used in reversed-phase liquid chromatography
Binding behaviour and conformational properties of globular proteins in the presence of immobilised non-polar ligands used in reversed-phase liquid chromatography
Engineering Village 2
? 2006 Elsevier Inc
Accession number: 05259172928
Title: Binding behaviour and conformational properties of globular proteins in the presence of immobilised non-polar ligands used in reversed-phase liquid chromatography
Authors: Boysen, Reinhard I.; Jong, Agnes J.O.; Hearn, Milton T.W.
Author affiliation: Australian Research Council Special Research Centre for Green Chemistry, Australian Centre for Research on Separation Science, Monash University, Clayton, Vic. 3800, Australia
Serial title: Journal of Chromatography A
Abbreviated serial title: J. Chromatogr. A
Volume: v 1079
Issue: n 1-2 SPEC. ISS.
Issue date: Jun 24 2005
Publication year: 2005
Pages: p 173-186
Language: English
ISSN: 0021-9673
CODEN: JCRAEY
Document type: Journal article (JA)
Publisher: Elsevier, Amsterdam, 1000 AE, Netherlands
Abstract: 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, ?H?assoc, ?S? assoc and ?C?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 whereby the corresponding free energy dependencies of globular proteins on association with solvated non-polar ligands in heterogeneous two-phase systems can be quantitatively evaluated in terms of fundamental molecular parameters.
Number of references: 64
Ei main heading: Liquid chromatography
Ei controlled terms: Proteins - Conformations - Thermodynamics - Enthalpy - Entropy
Uncontrolled terms: Non-polar ligands - Globular proteins - Cytochrome - Biophysical properties
Ei classification codes: 801 Chemistry - 804.1 Organic Compounds - 801.4 Physical Chemistry - 641.1 Thermodynamics
Treatment: Experimental (EXP)
DOI: 10.1016/j.chroma.2005.03.097
Database: Compendex
Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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