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The roles of residue position and charge in the cryoprotective behaviour of the Vitis riparia K2 and YSK2 dehydrins

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dc.contributor.advisor Graether, Steffen
dc.contributor.author Palmer, Sharall
dc.date.accessioned 2017-09-15T15:27:41Z
dc.date.available 2017-09-15T15:27:41Z
dc.date.copyright 2017-09
dc.date.created 2017-09-11
dc.date.issued 2017-09-15
dc.identifier.uri http://hdl.handle.net/10214/11598
dc.description.abstract Dehydrins are group II Late Embryogenesis Abundant proteins that accumulate in plants during seed development and in response to abiotic stresses. The biological function of dehydrins remain elusive, as they are multi-functional in vitro. The contribution of sequence and charge to the cryoprotective behaviour of dehydrins was analyzed using synthetic variants of the Vitis riparia YSK2 and K2 proteins: ScYSK2, a scrambled version of YSK2; and AntiK2, a charge-reversed version of K2. Circular dichroism (CD) spectroscopy analysis revealed that dehydrin-induced changes in the structure of YFH1 was dependent on sequence and independent of residue charge. An LDH cryoprotection assay showed that the efficiency of YSK2 was unrelated to its sequence, whereas the efficiency of K2 depended on its residue charge type. CD spectroscopy analysis also suggested that the mechanism of protein stabilization by dehydrins may be more like glycerol than polyethylene glycol. Identifying functionally important residues in dehydrins would provide insight into the potential mechanism(s) of their protective behaviour. en_US
dc.language.iso en en_US
dc.subject Dehydrins en_US
dc.subject Cryoprotection en_US
dc.title The roles of residue position and charge in the cryoprotective behaviour of the Vitis riparia K2 and YSK2 dehydrins en_US
dc.type Thesis en_US
dc.degree.programme Molecular and Cellular Biology en_US
dc.degree.name Master of Science en_US
dc.degree.department Department of Molecular and Cellular Biology en_US
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