Thermodynamic analysis of denatured lysozyme folded on moderately hydrophobic surface at 298 K

@article{Geng2009ThermodynamicAO,
  title={Thermodynamic analysis of denatured lysozyme folded on moderately hydrophobic surface at 298 K},
  author={X. Geng and H. Gao and Binglong Wang and A. Liu and X. Y. Feng},
  journal={Journal of Thermal Analysis and Calorimetry},
  year={2009},
  volume={95},
  pages={345-352}
}
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… Expand
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