Electrochemical modulation of sickle cell haemoglobin polymerisation
Sickle cell haemoglobin differs from normal haemoglobin by a single amino acid in its chain. This amino acid replacement, from glutamic acid to valine, causes polymerisation of proteins into defined long insoluble fibres with a typical diameter of 21.5 nm. The polymerisation is triggered by the form...
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University College London (University of London)
2008
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| Online Access: | http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.631782 |