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Determination of free energy of protein folding on liquid-solid interface


Based on the fact that the stoichiometric displacement model for retention of solute and the total adsorption free energy of solute on a solid surface can be divided into two components, net adsorption and net desorbed energies, a new principle and an equation for calculating the free energy of protein folding, ΔΔGF, on the solid surface are proposed. With high-performance hydrophobic interaction chromatography (HPHIC), an experimental method for determining the ΔΔGF is established. Lysozyme and α-amylase have been selected as examples to test the new method, and their ΔΔGF on the HPHIC stationary phase surface are found to be much higher than that reported from a solution. In addition, the ΔΔGF of the two proteins are found to increase with the concentration of denaturing agent employed. The average standard deviations, ±4.7% for lysozyme and ±3.0% for α-amylase, indicate that the new method has a satisfactory reproducibility and reliability.

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Correspondence to Xindu Geng.

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Geng, X., Zhang, J. & Wei, Y. Determination of free energy of protein folding on liquid-solid interface. Chin.Sci.Bull. 45, 237–241 (2000).

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  • stoichiometric displacement model
  • high-performance hydrophobic interaction chromatography
  • adsorption free energy
  • protein folding