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

determination of displacement adsorption enthalpies of protein refolding on
a moderately hydrophobic surface at 308 K},
  author={X. Geng and Y. Wu and B. H. Wang and H. Zhang and X. Geng and J. Xing},
  journal={Journal of Thermal Analysis and Calorimetry},
  • X. Geng, Y. Wu, +3 authors J. Xing
  • Published 2006
  • Chemistry
  • Journal of Thermal Analysis and Calorimetry
AbstractBoth 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… Expand
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Calorimetric determination of enthalpies of lysozyme folding at a liquid-solid interface
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Isothermal Titration Microcalorimetric Studies of the Effect of Temperature on Hydrophobic Interaction between Proteins and Hydrophobic Adsorbents.
  • Huang, Lin, Chen, Ruaan
  • Chemistry, Medicine
  • Journal of colloid and interface science
  • 2000
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