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10.1073/pnas.1415663111

http://scihub22266oqcxt.onion/10.1073/pnas.1415663111
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C4260602!4260602!25404291
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suck abstract from ncbi


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pmid25404291      Proc+Natl+Acad+Sci+U+S+A 2014 ; 111 (48): 17158-63
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  • Orientation of aromatic residues in amyloid cores: Structural insights into prion fiber diversity #MMPMID25404291
  • Reymer A; Frederick KK; Rocha S; Beke-Somfai T; Kitts CC; Lindquist S; Nordén B
  • Proc Natl Acad Sci U S A 2014[Dec]; 111 (48): 17158-63 PMID25404291show ga
  • Amyloids, which are protein fiber aggregates, are often associated with neurodegenerative diseases such as Alzheimer?s, but they can also be beneficial, as in yeasts, where they help cells adapt to environmental changes. Intriguingly, the same protein has the ability to aggregate into different fiber forms, known as strains, that generate distinct biological phenotypes. Structurally, little is known about strains. Using polarized light spectroscopy, we provide structural information on two distinct phenotypic strains of the yeast translation termination factor, Sup35. Remarkably, they show similar orientation of aromatic residues in the fiber core relative to the fiber direction, suggesting similar structures. Small variations are observed, indicating different local environments for aromatic residues outside the core, reflecting differences in fiber packing.
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