Journal of Thermal Analysis and Calorimetry
Volume/Issue:
Volume 95: Issue 2
Thermodynamic analysis of denatured lysozyme folded on moderately hydrophobic surface at 298 K
Authors:
X. Geng Xi’an Polytechnic University College of Environment and Chemical Engineering Xi’an 710048 China

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H. Gao Xi’an Polytechnic University College of Environment and Chemical Engineering Xi’an 710048 China

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B. Wang Peking University Institute of Physical Chemistry Beijing 100871 China

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A. Liu Xi’an Polytechnic University College of Environment and Chemical Engineering Xi’an 710048 China

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X. Feng Xi’an Polytechnic University College of Environment and Chemical Engineering Xi’an 710048 China

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Pages:
345–352
Online Publication Date:
12 Mar 2009
Publication Date:
01 Feb 2009
Article Category:
Research Article
DOI:
https://doi.org/10.1007/s10973-008-9231-8
Keywords:
adsorption; calorimetry; fractions of thermodynamic functions; hydrophobic surface; lysozyme; subprocesses of protein folding
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Abstract  

Both calorimetric determination of displacement adsorption enthalpies ΔH and measurement of adsorbed amounts of lysozyme (Lyz) denatured by 1.8 mol L−1 guanidine hydrochloride (GuHCl) on a moderately hydrophobic packings at 298 K, pH 7.0 and various salt concentrations were carried out. Based on the thermodynamics of stoichiometric displacement theory (SDT) the fractions of thermodynamic functions, which related to four subprocesses of denatured protein refolding on the surface, were calculated and thermodynamic analysis that which one of the subprocesses plays major role for contribution to the thermodynamic fractions was made in detail. The moderately hydrophobic surface can provide denatured Lyz energy and make it gain more conformation with surface coverage or salt concentration increment. The displacement adsorptions of denatured Lyz onto PEG-600 surface are exothermic, more structure-ordered and enthalpy driven processes.

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Cover Journal of Thermal Analysis and Calorimetry
Journal of Thermal Analysis and Calorimetry
Print ISSN:
1388-6150
Online ISSN:
1572-8943

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation		 1969
Volumes
per Year		 1
Issues
per Year		 24
Founder Akadémiai Kiadó
Founder's
Address		 H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address		 H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher		 Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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