[HTML][HTML] The same primary structure of the prion protein yields two distinct self-propagating states
N Makarava, IV Baskakov - Journal of Biological Chemistry, 2008 - ASBMB
The question of whether distinct self-propagating structures could be formed within the same
amino acid sequence in the absence of external cofactors or templates has important
implications for a number of issues, including the origin of prion strains and the engineering
of smart, self-assembling peptide-based biomaterials. In the current study, we showed that
chemically identical prion protein can give rise to conformationally distinct, self-propagating
amyloid structures in the absence of cellular cofactors, post-translational modification, or PrP …
amino acid sequence in the absence of external cofactors or templates has important
implications for a number of issues, including the origin of prion strains and the engineering
of smart, self-assembling peptide-based biomaterials. In the current study, we showed that
chemically identical prion protein can give rise to conformationally distinct, self-propagating
amyloid structures in the absence of cellular cofactors, post-translational modification, or PrP …