Orientation of aromatic residues in amyloid cores: structural insights into prion fiber diversity.

ABSTRACT: Structural conversion of one given protein sequence into different amyloid states, resulting in distinct phenotypes, is one of the most intriguing phenomena of protein biology. Despite great efforts the structural origin of prion diversity remains elusive, mainly because amyloids are insoluble yet noncrystalline and therefore not easily amenable to traditional structural-biology methods. We investigate two different phenotypic prion strains, weak and strong, of yeast translation termination factor Sup35 with respect to angular orientation of tyrosines using polarized light spectroscopy. By applying a combination of alignment methods the degree of fiber orientation can be assessed, which allows a relatively accurate determination of the aromatic ring angles. Surprisingly, the strains show i

SUBMITTER: Reymer A 

PROVIDER: S-EPMC4260602 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature