Exploring the accessible conformations of N-terminal acetylated α-synuclein

Alpha synuclein (αsyn) fibrils are found in the Lewy Bodies of patients with Parkinson’s disease (PD). The aggregation of the αsyn monomer to soluble oligomers and insoluble fibril aggregates is believed to be one of the causes of PD. Recently, the view of the native state of αsyn as a monomeric ens...

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Bibliographic Details
Published in:	FEBS letters Vol. 587; no. 8; pp. 1128 - 1138
Main Authors:	Moriarty, Gina M., Janowska, Maria K., Kang, Lijuan, Baum, Jean
Format:	Journal Article
Language:	English
Published:	England Elsevier B.V 17-04-2013
Subjects:	Ac-αsyn acetylated α-synuclein Acetylation Aggregation alpha-Synuclein - chemistry alpha-Synuclein - metabolism beta-octyl glucopyranoside BOG circular dichroism clear native PAGE CN-PAGE electrospray ionization-mass spectrometry electrospray ionization–ion mobility spectrometry-mass spectrometry ELISA Ensemble enzyme-linked immunosorbent assay ESI-MS ESI–IMS-MS Fibril Fibril-resistance glutathione S-transferase GST Humans IDP Intrinsically disordered protein Lewy Bodies - metabolism N-acetyltransferase N-acetyltransferase B NAC Nat NatB NMR non-amyloid component region nuclear magnetic resonance Oligomer Parkinson Disease - metabolism Parkinson Disease - pathology Parkinson's disease post-translational modifications Protein Conformation Protein Multimerization Protein Structure, Secondary PTM RBC red blood cells SE-AUC SEC sedimentation equilibrium-analytical ultracentrifugation size exclusion chromatography SLS static light scattering thioflavin T ThT α-Synuclein αsyn Nat ThT α-Synuclein NatB PTM CN-PAGE Oligomer SE-AUC Aggregation RBC Fibril-resistance IDP αsyn BOG SLS Acetylation CD GST ESI-MS Ac-αsyn SEC NAC NMR PD Ensemble ESI–IMS-MS Intrinsically disordered protein Parkinson’s disease ELISA Fibril
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