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http://eprints.org/relation/isVolatileVersionOf http://etheses.bham.ac.uk/id/document/3514 http://eprints.org/relation/ispreviewThumbnailVersionOf http://etheses.bham.ac.uk/id/document/3514 http://eprints.org/relation/isVersionOf http://etheses.bham.ac.uk/id/document/3514 archive 4031 disk0/00/00/14/83 2011-05-11 15:18:49 2019-01-23 09:54:17 2011-07-19 16:37:06 thesis show 0 Barry Christopher Harper Ramsden D. B. ftp://ubira.bham.ac.uk/eTheses/1483_Barry/ University of Birmingham unpub RC0321 30sch_medi Printing errors in the Appendix are in the original thesis. Cysteine Dioxygenase is an enzyme that catalyses the reaction of cysteine to cysteinesulfinic acid and is thought to regulate the intracellular concentrations of its substrate. The enzyme may also be involved in the oxidation of exposed sulfidrils of protein and by implication, involved in cell signalling or regulation. Substrate and products of cysteine dioxygenase are known to be disrupted in a number of neurodegenerative diseases making the protein an important target for medical research. To date, the structure of the protein has not been solved. An understanding of its structure and reaction mechanism will further the understanding of the aetiology of a number of different pathologies. Its structure may also further the development of novel pharmacological drugs. 2003 graduation 2325166 eng other Scanned by Hollingworth & Moss This unpublished thesis/dissertation is copyright of the author and/or third parties. The intellectual property rights of the author or third parties in respect of this work are as defined by The Copyright Designs and Patents Act 1988 or as modified by any successor legislation. Any use made of information contained in this thesis/dissertation must be in accordance with that legislation and must be properly acknowledged. Further distribution or reproduction in any format is prohibited without the permission of the copyright holder. public 203 University of Birmingham Department of Clinical Neuroscience d_ph na 2003 graduation