ParkinsonFranceV1, Main, Exploration, bibRecordById, pubmed:26318307

Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.

Identifieur interne : 000277 ( Main/Exploration ); précédent : 000276; suivant : 000278

Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.

Auteurs : Joeri Verasdonck [Suisse] ; Luc Bousset [France] ; Julia Gath [Suisse] ; Ronald Melki [France] ; Anja Böckmann [France] ; Beat H. Meier [Suisse]

Source :

Biomolecular NMR assignments [ 1874-270X ] ; 2016.

RBID : pubmed:26318307

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Hydrogen-Ion Concentration, Mice, Nuclear Magnetic Resonance, Biomolecular, Protein Isoforms (chemistry), Protein Structure, Secondary, alpha-Synuclein (chemistry).
MESH :
- chemical , chemistry : Protein Isoforms, alpha-Synuclein.
- Amino Acid Sequence, Animals, Hydrogen-Ion Concentration, Mice, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary.
mix :
- Polymorphism , Synuclein, Solid-state NMR .

Abstract

Polymorphism is a common and important phenomenon for protein fibrils which has been linked to the appearance of strains in prion and other neurodegenerative diseases. Parkinson disease is a frequently occurring neurodegenerative pathology, tightly associated with the formation of Lewy bodies. These deposits mainly consist of α-synuclein in fibrillar, β-sheet-rich form. α-synuclein is known to form numerous different polymorphs, which show distinct structural features. Here, we describe the chemical shift assignments, and derive the secondary structure, of a polymorph that was fibrillized at higher-than-physiological pH conditions. The fibrillar core contains residues 40-95, with both the C- and N-terminus not showing any ordered, rigid parts. The chemical shifts are similar to those recorded previously for an assigned polymorph that was fibrillized at neutral pH.

Url:

https://hal.archives-ouvertes.fr/hal-01240180

DOI: 10.1007/s12104-015-9628-9
PubMed: 26318307

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">Polymorphism is a common and important phenomenon for protein fibrils which has been linked to the appearance of strains in prion and other neurodegenerative diseases. Parkinson disease is a frequently occurring neurodegenerative pathology, tightly associated with the formation of Lewy bodies. These deposits mainly consist of α-synuclein in fibrillar, β-sheet-rich form. α-synuclein is known to form numerous different polymorphs, which show distinct structural features. Here, we describe the chemical shift assignments, and derive the secondary structure, of a polymorph that was fibrillized at higher-than-physiological pH conditions. The fibrillar core contains residues 40-95, with both the C- and N-terminus not showing any ordered, rigid parts. The chemical shifts are similar to those recorded previously for an assigned polymorph that was fibrillized at neutral pH.</div>
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La maladie de Parkinson en France (serveur d'exploration)

Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.

Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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	La maladie de Parkinson en France (serveur d'exploration)
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