Characterisation of Thioredoxin Dimers: A Biochemical Study
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In addition to the conserved active site cysteines that are responsible for the classical redox activity of thioredoxins (Trx’s), vertebrate Trx’s contain an additional three conserved cysteines at position 62, 69 and 73. These structural cysteines are known to be subjected to a variety of post translational modifications including dimerisation that are believed to contribute to the regulation and diversity of function of vertebrate Trx’s. Reports of the formation of “disulphide linked dimers” have been a long standing observation since the earliest studies on vertebrate Trx’s, however detailed studies on dimerisation have been limited in number and the extent of characterisation achieved. Despite the potential for a diversity of dimeric forms with different structural and functional properties there has been a common assumption arising from the literature (despite some evidence to the contrary) that all dimers so far described are much the same and all are redox inactive.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Physical Science
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Human Trx dimerisation