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Evaluation of Copper(2+) Affinities for the Prion Protein


Reference:

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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Official URL:

http://dx.doi.org/10.1021/bi9011397

Abstract

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.

Details

Item Type Articles
CreatorsNadal, R. C., Davies, P., Brown, D. R. and Viles, J. H.
DOI10.1021/bi9011397
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code16151

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