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dc.contributor.authorHerzog, G.
dc.contributor.authorNolan, M.
dc.contributor.authorArrigan, Damien
dc.date.accessioned2017-01-30T11:51:22Z
dc.date.available2017-01-30T11:51:22Z
dc.date.created2011-11-18T01:21:25Z
dc.date.issued2011
dc.identifier.citationHerzog, Gregoire and Nolan, Marie-Therese and Arrigan, Damien. 2011. Haemoglobin unfolding studies at the liquid-liquid interface. Electrochemistry Communications. 13 (7): pp. 723-725.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/15701
dc.identifier.doi10.1016/j.elecom.2011.04.020
dc.description.abstract

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.

dc.publisherElsevier
dc.subjecturea
dc.subjecthaemoglobin
dc.subjectprotein unfolding
dc.subjectITIES
dc.subjectCyclic voltammetry
dc.titleHaemoglobin unfolding studies at the liquid-liquid interface
dc.typeJournal Article
dcterms.source.volume13
dcterms.source.startPage723
dcterms.source.endPage725
dcterms.source.issn13882481
dcterms.source.titleElectrochemistry Communications
curtin.note

NOTICE: This is the author's version of a work that was accepted for publication in Electrochemistry Communications. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Electrochemistry Communications, 13, 7, 2011. DOI: 10.1016/j.elecom.2011.04.020

curtin.departmentNanochemistry Research Institute (Research Institute)
curtin.accessStatusOpen access


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