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Article

Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity.

Biochimica et biophysica acta. Proteins and proteomics - 1 Sept 2020

Okuwaki Rina, Shinmura Iori, Morita Shiki, Matsugami Akimasa, Hayashi Fumiaki, Goto Yuji, Nishimura Chiaki

Abstract excerpt

The residual solution structures of two alpha-synuclein mutants, A30P and A53T, observed in family members of patients with Parkinson's disease were compared with that of wild-type by NMR. The A53T substitution had been shown to accelerate fibril formation of alpha-synuclein, whereas the A30P mutation has the negative and positive effects on the formation of the fibril and spherical oligomer, respectively. The...

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PMID: 32497661
DOI: 10.1016/j.bbapap.2020.140464

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