ESR Spectroscopy Investigation of the Denaturation Process of Soybean Peroxidase Induced by Guanidine Hydrochloride, DMSO or Heat |
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Authors: | Barbara Boscolo Enzo Laurenti Elena Ghibaudi |
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Affiliation: | (1) Dip. Chimica I.F.M., Università di Torino, Via Giuria 7, 10125 Torino, Italy |
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Abstract: | The involvement of protein denaturation and/or misfolding processes in the insurgence of several diseases raises the interest in structural dynamic studies of proteins. The use of nitroxide spin labels with electron paramagnetic resonance is a powerful tool for detecting structural changes in proteins. In the present study, we apply this strategy to soybean peroxidase (SBP), a protein characterised by high thermal and structural stability, and we propose a simple method to analyse the anisotropy changes of the protein system and to relate them with the structural changes induced by protein unfolding. We examined the effect of temperature, guanidine hydrochloride and dimethylsulfoxide on the stability of SBP and looked for correlations between the ESR results and the experimental findings obtained by other techniques, reported in the literature. The agreement between data obtained through different strategies supports the validity and reliability of the ESR approach to protein unfolding. |
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Keywords: | Peroxidase ESR spectroscopy spin label protein folding anisotropy |
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