The relative and regional stabilities of the hamster, mouse, rabbit and bovine prion proteins towards urea unfolding assessed by NMR and CD spectroscopies.
The relative and regional stabilities of the hamster, mouse, rabbit and bovine prion proteins towards urea unfolding assessed by NMR and CD spectroscopies.
The relative and regional stabilities of the hamster, mouse, rabbit and bovine prion proteins towards urea unfolding assessed by NMR and CD spectroscopies.
Biochemistry. 2011 Jul 29;
Authors: Julien O, Chatterjee S, Bjorndahl TC, Sweeting B, Acharya S, Semenchenko V, Chakrabartty A, Pai EF, Wishart DS, Sykes BD, Cashman NR
The residue specific urea-induced unfolding patterns of recombinant prion proteins from different species (bovine, rabbit, mouse, and Syrian hamster) were monitored using high-resolution 1H nuclear magnetic resonance (NMR) spectroscopy. Protein constructs of different lengths, and with and without a His-tag attached at the N-terminus, were studied. The various species showed different overall sensitivity towards urea denaturation with stabilities in the order, hamster
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The relative and regional stabilities of the hamster, mouse, rabbit and bovine prion proteins towards urea unfolding assessed by NMR and CD spectroscopies.
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