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Journal article

Inter-oligomer interactions of the human prion protein are modulated by the polymorphism at codon 129.

Abstract:

The common polymorphism at codon 129 in the human prion protein (PrP) has been shown in many studies to influence not only the pathology of prion disease but also the misfolding propensity of PrP. Here we used NMR, CD and atomic force microscopy in solution to investigate differences in beta-oligomer (beta(O)) formation and inter-oligomer interaction depending on the polymorphism at codon 129. NMR investigations assigned the observable amide resonances to the beta(O) N-terminal segments, show...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2008.05.057

Authors


Voitchovsky, K More by this author
Mitchel, C More by this author
Tahiri-Alaoui, A More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Physics, Condensed Matter Physics
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Journal:
Journal of molecular biology
Volume:
381
Issue:
1
Pages:
212-220
Publication date:
2008-08-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:5527481f-819c-4dae-bdd6-b696fede288d
Source identifiers:
30494
Local pid:
pubs:30494

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