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Dokumenttyp:
Journal Article; Article
Autor(en):
Whyte, SM; Sylvester, ID; Martin, SR; Gill, AC; Wopfner, F; Schätzl, HM; Dodson, GG; Bayley, PM
Titel:
Stability and conformational properties of doppel, a prion-like protein, and its single-disulphide mutant.
Abstract:
Both prion protein and the structurally homologous protein doppel are associated with neurodegenerative disease by mechanisms which remain elusive. We have prepared murine doppel, and a mutant with one of the two disulphide bonds removed, in the expectation of increasing the similarity of doppel to prion protein in terms of conformation and stability. Unfolding studies of doppel and the mutant have been performed using far-UV CD over a range of solution conditions known to favour the alpha-->bet...     »
Zeitschriftentitel:
Biochem J
Jahr:
2003
Band / Volume:
373
Heft / Issue:
Pt 2
Seitenangaben Beitrag:
485-94
Sprache:
eng
Volltext / DOI:
doi:10.1042/BJ20021911
PubMed:
http://view.ncbi.nlm.nih.gov/pubmed/12665426
Print-ISSN:
0264-6021
TUM Einrichtung:
Institut für Virologie
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