| Summary: | The electrochemical behaviour of haemoglobin denatured using different concentrations of urea was investigated at the liquid|liquid interface. The reverse peak current varied with the concentration of urea, allowing the building of the unfolding curve, which compares well with UV-Vis absorbance results. Thermodynamic parameters, such as the change in free energy of folding in water, , and the index of the compactness of the protein, m, were extracted from the experimental data. The work here presents a simple electrochemical method for the study of protein unfolding by electrochemistry at the liquid | liquid interface.
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