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

Anna Reymer (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; K. K. Frederick ; Sandra Rocha (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; Tamas Beke-Somfai (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; Catherine Kitts (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; S. Lindquist ; Bengt Nordén (Institutionen för kemi- och bioteknik, Fysikalisk kemi)
Proceedings of the National Academy of Sciences of the United States of America (0027-8424). Vol. 111 (2014), 48, p. 17158-17163.
[Artikel, refereegranskad vetenskaplig]

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 identical average orientations of the tyrosines, which are evenly spread through the amyloid core. Small variations between the two strains are related to the local environment of a fraction of tyrosines outside the core, potentially reflecting differences in fibril packing.

Nyckelord: linear dichroism, polarized light, prion proteins, Sup35 strains, tyrosine



Denna post skapades 2015-01-07. Senast ändrad 2015-01-27.
CPL Pubid: 209793

 

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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Fysikalisk kemi (2005-2014)

Ämnesområden

Biofysikalisk kemi

Chalmers infrastruktur

 


Projekt

Denna publikation är ett resultat av följande projekt:


Supramolecular motive power (SUMO) (EC/FP7/227700)