ArticleJournal of biomolecular NMR2006
13C, 15N resonance assignment of parts of the HET-s prion protein in its amyloid form.
Article in Journal of biomolecular NMR, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 91 citations in OpenAlex.
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- Protein resonance assignment by solid-state NMR based onJournal of biomolecular NMR · 2021Article
- Advances in studying protein disorder with solid-state NMR.Solid state nuclear magnetic resonance · 2020Review
- Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.Methods (San Diego, Calif.) · 2018Review
- Detection of side-chain proton resonances of fully protonated biosolids in nano-litre volumes by magic angle spinning solid-state NMR.Journal of biomolecular NMR · 2018Article
- Afterglow Solid-State NMR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Study of Amyloids Using Yeast.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Partially-deuterated samples of HET-s(218-289) fibrils: assignment and deuterium isotope effect.Journal of biomolecular NMR · 2017Article
- INFOS: spectrum fitting software for NMR analysis.Journal of biomolecular NMR · 2017Article
- Characterization of fibril dynamics on three timescales by solid-state NMR.Journal of biomolecular NMR · 2016Article
- Prions are affected by evolution at two levels.Cellular and molecular life sciences : CMLS · 2016Review
- On the problem of resonance assignments in solid state NMR of uniformly ¹⁵N,¹³C-labeled proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015Review
- Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution.International journal of nanomedicine · 2015Article
- Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289).The Journal of biological chemistry · 2013Article
- Efficient band-selective homonuclear CO-CA cross-polarization in protonated proteins.Journal of biomolecular NMR · 2013Article
- Automated solid-state NMR resonance assignment of protein microcrystals and amyloids.Journal of biomolecular NMR · 2013Article
- The mechanism of toxicity in HET-S/HET-s prion incompatibility.PLoS biology · 2012Article
- Study of amyloids using yeast.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion.Journal of biomolecular NMR · 2011Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The partial 15N and 13C solid-state NMR resonance assignment of the HET-s prion protein fragment 218-289 in its amyloid form is presented. It is based on experiments measured at MAS frequencies in the range of 20-40 kHz using exclusively adiabatic polarization-transfer schemes. The resonance assignment within each residue is based on two-dimensional 13C-13C correlation spectra utilizing the DREAM mixing scheme. The sequential linking of the assigned residues used a set of two- and three-dimensional 15N-13C correlation experiments. Almost all cross peaks visible in the spectra are assigned, but only resonances from 43 of the 78 amino-acid residues could be detected. The missing residues are thought to be highly disordered and/or highly dynamic giving rise to broad resonance lines that escaped detection in the experiments applied. The line widths of the observed resonances are narrow and comparable to line widths observed in micro-crystalline samples. The 43 assigned residues are located in two fragments of about 20 residues.
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