N-terminal acetylation of α-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer

The conformational properties of soluble α-synuclein, the primary protein found in patients with Parkinson's disease, are thought to play a key role in the structural transition to amyloid fibrils. In this work, we report that recombinant 100% N-terminal acetylated α-synuclein purified under mi...

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Main Authors: Kang, Lijuan, Moriarty, Gina M, Woods, Lucy A, Ashcroft, Alison E, Radford, Sheena E, Baum, Jean
Formato: Artigo
Idioma:Inglês
Publicado: Wiley Subscription Services, Inc., A Wiley Company 2012
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Accelerated Communication
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC3403430/
https://ncbi.nlm.nih.gov/pubmed/22573613
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.2088
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