ArticleBiochemistry2010
Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Covalently PD-L1 Anchoring Drives Bispecific Nanostructure Assembly for Spatial Control of T Cell Recruitment and Activation.Angewandte Chemie (International ed. in English) · 2026Article
- Aggregation of Amyloid-like Peptides in Different Solvents.Journal of molecular liquids · 2026Article
- Atomic Structure of GNNQQNY Nanocrystals: A Validated Approach for Polymorphic Amyloids.The journal of physical chemistry letters · 2025Article
- Structural Insights Into Amyloid Polymorphism: The Impact of Glutamine to Norleucine Substitutions in GNNQQNY Aggregation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Homonuclear J-couplings and heteronuclear structural constraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Structural characterization of E22G AβPhysical chemistry chemical physics : PCCP · 2024Article
- Solid-state nuclear magnetic resonance in the structural study of polyglutamine aggregation.Biochemical Society transactions · 2024Review
- Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural Arrangement within a Peptide Fibril Derived from the Glaucoma-Associated Myocilin Olfactomedin Domain.The journal of physical chemistry. B · 2021Article
- Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy.Frontiers in molecular biosciences · 2021Review
- Clustering and Fibril Formation during GNNQQNY Aggregation: A Molecular Dynamics Study.Biomolecules · 2020Article
- Glutamine Side ChainJournal of the American Chemical Society · 2019Article
- Functional Amyloid and Other Protein Fibers in the Biofilm Matrix.Journal of molecular biology · 2018Review
- Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.Biophysical reviews · 2018Review
- Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.The journal of physical chemistry. B · 2018Article
- Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Solid state nuclear magnetic resonance · 2017Review
- 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
- On the use of ultracentrifugal devices for routine sample preparation in biomolecular magic-angle-spinning NMR.Journal of biomolecular NMR · 2017Article
- Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Quarterly reviews of biophysics · 2017Review
- Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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3 authors.
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Abstract
Several human diseases are associated with the formation of amyloid aggregates, but experimental characterization of these amyloid fibrils and their oligomeric precursors has remained challenging. Experimental and computational analysis of simpler model systems has therefore been necessary, for instance, on the peptide fragment GNNQQNY7−13 of yeast prion protein Sup35p. Expanding on a previous publication, we report here a detailed structural characterization of GNNQQNY fibrils using magic angle spinning (MAS) NMR. On the basis of additional chemical shift assignments we confirm the coexistence of three distinct peptide conformations within the fibrillar samples, as reflected in substantial chemical shift differences. Backbone torsion angle measurements indicate that the basic structure of these coexisting conformers is an extended β-sheet. We structurally characterize a previously identified localized distortion of the β-strand backbone specific to one of the conformers. Intermolecular contacts are consistent with each of the conformers being present in its own parallel and in-register sheet. Overall the MAS NMR data indicate a substantial difference between the structure of the fibrillar and crystalline forms of these peptides, with a clearly increased complexity in the GNNQQNY fibril structure. These experimental data can provide guidance for future work, both experimental and theoretical, and provide insights into the distinction between fibril growth and crystal formation.
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