ArticleProceedings of the National Academy of Sciences of the United States of America2014
Orientation of aromatic residues in amyloid cores: structural insights into prion fiber diversity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Orientation of α-Synuclein at Negatively Charged Lipid Vesicles: Linear Dichroism Reveals Time-Dependent Changes in Helix Binding Mode.Journal of the American Chemical Society · 2021Article
- Prediction of Transmembrane Regions, Cholesterol, and Ganglioside Binding Sites in Amyloid-Forming Proteins Indicate Potential for Amyloid Pore Formation.Frontiers in molecular neuroscience · 2021Article
- Michler's hydrol blue elucidates structural differences in prion strains.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A Decentralized Approach to the Formulation of Hypotheses: A Hierarchical Structural Model for a Prion Self-Assembled System.Scientific reports · 2016Article
- UV-Vis spectroscopy of tyrosine side-groups in studies of protein structure. Part 1: basic principles and properties of tyrosine chromophore.Biophysical reviews · 2016Review
- The Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules.Cell · 2016Review
- Light and heat control over secondary structure and amyloid-like fiber formation in an overcrowded-alkene-modified Trp zipper.Chemical science · 2015Article
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Authors and funding
7 authors.
Funding
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 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.
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Registered trials
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