Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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 and M. M. Santoro

Volume 10, Issue 1, 2003

Page: [73 - 81] Pages: 9

DOI: 10.2174/0929866033408336

Price: $65

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


Rights & Permissions Print Export Cite as
© 2022 Bentham Science Publishers | Privacy Policy