DENATURED THERMODYNAMICS FOR PROTEINS IN HYDROPHOBIC INTERACTION CHROMATOGRAPHY

The thermodynamic behaviors for some proteins and small molecules in h ydrophobic interaction chromatography are studied in the temperature r ange of 21 similar to 80 degrees C. The thermodynamic parameters (Delt a H degrees, Delta S degrees, Delta G degrees) of these proteins are d etermined by using Van't Hoff relationship (lnk'- 1/T). By using the o btained standard entropy change (Delta S degrees) and free energy chan ge (Delta G degrees), the conformational change of the proteins is jud ged in chromatographic process. The linear relationships between Delta H degrees and Delta S degrees can be used to evaluate ''compensation temperature'' (beta) at the protein denaturation and identify the iden tity of the protein retention mechanism in hydrophobic interaction chr omatography.