NDLI: Microcalorimetric determination of displacement adsorption enthalpies of protein refolding on a moderately hydrophobic surface at 308 K

Content Provider	Springer Nature Link
Author	Geng, X. P. Wu, Y. N. Wang, B. H. Zhang, H. F. Geng, X. D. Xing, J. W.
Copyright Year	2006
Abstract	Both microcalorimetric determination of displacement adsorption enthalpies ΔH and measurement of adsorbed amounts of guanidine – denatured lysozyme (Lys) refolding on the surface of hydrophobic interaction chromatography (HIC) packings at 308 K were carried out and compared with that at 298 K. Study shows that both temperature and concentration of guanidine hydrochloride (GuHCl) affect the molecular mechanism of hydrophobic interaction of protein with adsorbent based on the analysis of dividing ΔH values into three kinds of enthalpy fractions. The adsorption in higher concentrations of GuHCl (>1.3 mol L$^{–1}$) at 308 K is an enthalpy-driving process, and the adsorption under other GuHCl concentrations is an entropy-driving process. The fact that the Lys denatured by 1.8 mol L$^{–1}$ GuHCl forms a relatively stable intermediate state under the studied conditions will not be changed by temperature.
Starting Page	601
Ending Page	608
Page Count	8
File Format	PDF
ISSN	13886150
Journal	Journal of thermal analysis
Volume Number	85
Issue Number	3
e-ISSN	15728943
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2006-08-31
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	displacement adsorption enthalpy hydrophobic interaction mechanism liquid/solid system lysozyme microcalorimetry protein folding Inorganic Chemistry Physical Chemistry Polymer Sciences Measurement Science, Instrumentation
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry Condensed Matter Physics

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