Article
Stability and conformational properties of doppel, a prion-like protein, and its single-disulphide mutant.
The Biochemical journal - 15 Jul 2003
Whyte Sheena M, Sylvester Ian D, Martin Stephen R, Gill Andrew C, Wopfner Franziska, Schätzl Hermann M, Dodson Guy G, Bayley Peter M
Abstract excerpt
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...
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