The Denaturation of α, β and Ψ Bovine Trypsin at Ph 3.0: Evidence of Intermediates
Authors: Martins, N.F.; Ferreira, E.; Torres, K.C.; Santoro, M.M.
Source: Protein and Peptide Letters, Volume 10, Number 1, February 2003 , pp. 73-81(9)
Publisher: Bentham Science Publishers
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 Ψforms suggest a molten globule state.
Document Type: Review Article
Publication date: February 1, 2003
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