Evaluation of Copper(2+) Affinities for the Prion Protein
Nadal, R. C., Davies, P., Brown, D. R. and Viles, J. H., 2009. Evaluation of Copper(2+) Affinities for the Prion Protein. Biochemistry, 48 (38), pp. 8929-8931.
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The prion protein (PrP) is a cell-surface Cu2+ binding glcoprotein which call bind six copper ions. The role of Cu2+ in PrP function, misfolding, and prion disease has generated much interest; however, the field has been hampered by a lack of consensus with regard to the affinity of Cu2+ for PrPC. Here we build on our understanding of the appearance of visible CD spectra for full-length PrP and fragments to determine the affinity of Cu2+ for four different binding modes, with dissociation constants ranging between 13 and 66 nM at pH 7.4.
|Creators||Nadal, R. C., Davies, P., Brown, D. R. and Viles, J. H.|
|Departments||Faculty of Science > Biology & Biochemistry|
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