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Studies on the conformational change of adsorbed BSA onto a moderately hydrophobic surface at different denaturant concentrations and surface coverages.
TLDR
The results showed that the surface can provide energy to denatured BSA and make it gain a more ordered conformation with GuHCl concentration increment and their tertiary structure may be more perfect with surface coverage increment. Expand
Fractions of thermodynamic functions for native lysozyme adsorption onto moderately hydrophobic surface
Calorimetric measurement of adsorption enthalpies of native lysozyme(Lyz) on a moderately hydrophobic surface at 25°C, pH 7.0 and various salt concentrations was performed. Based on theExpand
Effect of salt concentrations on the displacement adsorption enthalpies of denatured protein folding at a moderately hydrophobic surface
AbstractThe displacement adsorption enthalpies (ΔH) of the refolding of lysozyme (Lys) denatured by 1.8 mol L–1 guanidine hydrochloride (GuHCl) on a moderately hydrophobic surface at 298 K, pH 7.0Expand
Calorimetric determination of enthalpies of lysozyme folding at a liquid-solid interface
SummaryCalorimetric determination of the total enthalpy changes (ΔHi) of guanidine-denatured lysozyme (Lys) during the adsorption with simultaneously refolding on the surface of hydrophobicExpand
Study on the fractions of thermodynamic function changes for both adsorption and desorption from a liquid-solid system☆☆☆
Abstract On the basis of the thermodynamics of the stoichiometric displacement model for adsorption of a solute, two equations to calculate separately two fractions of the Gibbs free energy for theExpand
Microcalorimetric determination of displacement adsorption enthalpies of protein refolding on a moderately hydrophobic surface at 308 K
AbstractBoth microcalorimetric determination of displacement adsorption enthalpies ΔH and measurement of adsorbed amounts of guanidine – denatured lysozyme (Lys) refolding on the surface ofExpand
Microcalorimetric study on conformational change of denatured RNase A adsorbed onto a moderately hydrophobic surface
Abstract The microcalorimetric method was used to measure the displacement adsorption heat of denatured (by 1.8 mol L−1 guanidine hydrochloride (GuHCl)) Ribonuclease A (RNase A) adsorbed onto aExpand
Adsorption enthalpy and desorption enthalpy during displacement of adsorbate to solvent in a liquid-solid system
The adsorption heat of the stoichiometric displacement process for the adsorption of a solute in a liquid-solid system was investigated. On the basis of the SDM-A and the rule of the additivity ofExpand
Thermodynamic analysis of denatured lysozyme folded on moderately hydrophobic surface at 298 K
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 moderatelyExpand
[DSC and FTIR study of adsorbed lysozyme on hydrophobic surface].
TLDR
Temperature due to endothermic peaks was reduced and the disturbance increased at higher temperature with the increase in salt concentration and surface coverage of adsorbed protein, which resulted in structural loss of advertisersorbed native lysozyme, whose performance was less stable. Expand
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