Solid-state NMR sequential assignments of the amyloid core of Sup35pNM
| Autor: | Birgit Habenstein, Anja Böckmann, Beat H. Meier, Anne K. Schütz, Luc Bousset, Yannick Sourigues, Nina Luckgei, Ronald Melki |
|---|---|
| Přispěvatelé: | Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Physical Chemistry [ETH Zürich], Department of Chemistry and Applied Biosciences [ETH Zürich] (D-CHAB), Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich)- Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich), Institut des Neurosciences Paris-Saclay (NeuroPSI), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Amyloid
Saccharomyces cerevisiae Proteins [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology Molecular Sequence Data Saccharomyces cerevisiae Fibril Biochemistry Structural Biology Amino Acid Sequence Nuclear Magnetic Resonance Biomolecular Peptide sequence Protein secondary structure chemistry.chemical_classification biology [SDV.NEU.PC]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Psychology and behavior Chemical shift [SDV.NEU.SC]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Cognitive Sciences biology.organism_classification Sup35pNM Fibrils Solid-state NMR Assignments Secondary structure 3. Good health Amino acid Crystallography chemistry Solid-state nuclear magnetic resonance Peptide Termination Factors |
| Zdroj: | Biomolecular NMR Assignments Biomolecular NMR Assignments, Springer, 2014, 8 (2), pp.365-70. ⟨10.1007/s12104-013-9518-y⟩ Biomolecular NMR Assignments, 8 (2) Biomolecular NMR assignments |
| ISSN: | 1874-270X |
| DOI: | 10.1007/s12104-013-9518-y⟩ |
| Popis: | Sup35pNM represents the N-terminal and middle (M) domains of the yeast Saccharomyces cerevisiae prion Sup35p. This fragment is commonly used for structural and functional studies of Sup35p. We here present a solid-state NMR study of fibrils formed by this fragment and show that sequential assignments can be obtained for the rigid and well-ordered parts of the protein using 3D spectroscopy. We describe in detail the sequential assignment of the 22 residues yielding strong, narrow signals with chemical shifts that correspond mostly to β-sheet secondary-structured amino acids that form the fibril core. ISSN:1874-270X ISSN:1874-2718 |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink