Haemoglobin unfolding studies at the liquid-liquid interface
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 resu...
| Main Authors: | , , |
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| Format: | Journal Article |
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Elsevier
2011
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| Online Access: | http://hdl.handle.net/20.500.11937/15701 |
| _version_ | 1848748965509464064 |
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| author | Herzog, G. Nolan, M. Arrigan, Damien |
| author_facet | Herzog, G. Nolan, M. Arrigan, Damien |
| author_sort | Herzog, G. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-14T07:13:25Z |
| format | Journal Article |
| id | curtin-20.500.11937-15701 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T07:13:25Z |
| publishDate | 2011 |
| publisher | Elsevier |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-157012019-02-19T04:25:52Z Haemoglobin unfolding studies at the liquid-liquid interface Herzog, G. Nolan, M. Arrigan, Damien urea haemoglobin protein unfolding ITIES Cyclic voltammetry 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. 2011 Journal Article http://hdl.handle.net/20.500.11937/15701 10.1016/j.elecom.2011.04.020 Elsevier fulltext |
| spellingShingle | urea haemoglobin protein unfolding ITIES Cyclic voltammetry Herzog, G. Nolan, M. Arrigan, Damien Haemoglobin unfolding studies at the liquid-liquid interface |
| title | Haemoglobin unfolding studies at the liquid-liquid interface |
| title_full | Haemoglobin unfolding studies at the liquid-liquid interface |
| title_fullStr | Haemoglobin unfolding studies at the liquid-liquid interface |
| title_full_unstemmed | Haemoglobin unfolding studies at the liquid-liquid interface |
| title_short | Haemoglobin unfolding studies at the liquid-liquid interface |
| title_sort | haemoglobin unfolding studies at the liquid-liquid interface |
| topic | urea haemoglobin protein unfolding ITIES Cyclic voltammetry |
| url | http://hdl.handle.net/20.500.11937/15701 |