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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...
Tallennettuna:
| Päätekijät: | , , , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Wiley Subscription Services, Inc., A Wiley Company
2012
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| Aiheet: | |
| Linkit: | 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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