Abstract

The conformational stability and the folding process of α, β and Ψ bovine trypsin at pH 3.0 followed by circular dichroism (CD) and size exclusion in HPLC have been analyzed as a function of urea concentration. The thermodynamic stability for α and β are ΔG = 15.91 ± 0.28 kcal / mol, DG = 15.54 ± 2.39 kcal / mol. respectively, and Ψ trypsin is ΔG = 16.10 ± 2.51 kcal / mol. The transition curves for α, β and Ψ forms suggest a molten globule state.

Keywords: trypsin, protein denaturation, thermodynamic stability, intermediates, molten globule