Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Biomolecular NMR Assignments Année : 2016

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

Résumé

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.
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Dates et versions

hal-01240180 , version 1 (08-12-2015)

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Joeri Verasdonck, Luc Bousset, Julia Gath, Ronald Melki, Anja Böckmann, et al.. Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.. Biomolecular NMR Assignments, 2016, 10 (1), pp.5-12. ⟨10.1007/s12104-015-9628-9⟩. ⟨hal-01240180⟩
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