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

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

Journal Name: Protein & Peptide Letters

Volume 10 , Issue 1 , 2003

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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

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Article Details

VOLUME: 10
ISSUE: 1
Year: 2003
Page: [73 - 81]
Pages: 9
DOI: 10.2174/0929866033408336

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