title: The denaturation of alpha, beta and psi bovine trypsin at pH 3.0: evidence of intermediates.
abstract: The conformational stability and the folding process of alpha, beta and Psi 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 a and b are deltaG = 15.91 +/- 0.28 kcal/mol, deltaG = 15.54 +/- 2.39 kcal/mol. respectively, and y trypsin is deltaG = 16.10 +/- 2.51 kcal/mol. The transition curves for alpha, beta and Psi forms suggest a molten globule state.
authors.affiliation: EMBRAPA - Genetic Resources and Biotechnology, Bioinformatics Laboratory, Parque Estação Biológica, Final Av. W/5 Norte Braslília, Brazil. natalia@cenargen.embrapa.br
authors.forename: N F
authors.initials: NF
authors.lastname: Martins
authors.forename: E
authors.initials: E
authors.lastname: Ferreira
authors.forename: K C L
authors.initials: KC
authors.lastname: Torres
authors.forename: M M
authors.initials: MM
authors.lastname: Santoro
mesh_terms: D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel / Q000379:methods; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013816:Thermodynamics; D014357:Trypsin / Q000737:chemistry* / Q000145:classification; D014508:Urea / Q000737:chemistry
chemical_list: D014508:Urea; D014357:Trypsin