The Denaturation of α, β and Ψ Bovine Trypsin at Ph 3.0: Evidence of Intermediates

Title: The Denaturation of α, β and Ψ Bovine Trypsin at Ph 3.0: Evidence of Intermediates

Volume: 10 Issue: 1

Author(s): N. F. Martins, E. Ferreira, K. C. L. Torres and M. M. Santoro

Affiliation:

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

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.

Cite this article as:

Martins F. N., Ferreira E., Torres C. L. K. and Santoro M. M., The Denaturation of α, β and Ψ Bovine Trypsin at Ph 3.0: Evidence of Intermediates, Protein & Peptide Letters 2003; 10 (1) . https://dx.doi.org/10.2174/0929866033408336