ParkinsonFranceV1, PubMed, Corpus, bibRecord, 000163

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

Identifieur interne : 000163 ( PubMed/Corpus ); précédent : 000162; suivant : 000164

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

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

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.

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.

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

Links to Exploration step

pubmed:26318307

Le document en format XML

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<author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name>
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<author><name sortKey="Gath, Julia" sort="Gath, Julia" uniqKey="Gath J" first="Julia" last="Gath">Julia Gath</name>
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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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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 to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki