The denaturation of alpha,beta and psi bovine trypsin at pH 3.0: evidence of intermediates |
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| Authors: | Martins N F Ferreira E Torres K C L Santoro M M |
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| Institution: | EMBRAPA - Genetic Resources and Biotechnology, Bioinformatics Laboratory, Parque Esta??o Biológica, Final Av. W/5 Norte Braslília, Brazil. natalia@cenargen.embrapa.br |
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| 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. |
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