哺乳动物Y145Stop朊病毒蛋白淀粉样原纤维的碳和氮化学位移归属
C and N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils.
作者信息
Theint Theint, Nadaud Philippe S, Surewicz Krystyna, Surewicz Witold K, Jaroniec Christopher P
机构信息
Department of Chemistry and Biochemistry, The Ohio State University, 222 CBEC Building, 151 West Woodruff Avenue, Columbus, OH, 43210, USA.
Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106, USA.
出版信息
Biomol NMR Assign. 2017 Apr;11(1):75-80. doi: 10.1007/s12104-016-9723-6. Epub 2016 Dec 21.
Abstract
The Y145Stop prion protein (PrP23-144), which has been linked to the development of a heritable prionopathy in humans, is a valuable in vitro model for elucidating the structural and molecular basis of amyloid seeding specificities. Here we report the sequential backbone and side-chain C and N assignments of mouse and Syrian hamster PrP23-144 amyloid fibrils determined by using 2D and 3D magic-angle spinning solid-state NMR. The assigned chemical shifts were used to predict the secondary structures for the core regions of the mouse and Syrian hamster PrP23-144 amyloids, and the results compared to those for human PrP23-144 amyloid, which has previously been analyzed by solid-state NMR techniques.
摘要
Y145Stop朊病毒蛋白（PrP23 - 144）与人类遗传性朊病毒病的发生有关，是用于阐明淀粉样蛋白种子特异性的结构和分子基础的重要体外模型。在此，我们报告了通过使用二维和三维魔角旋转固态核磁共振确定的小鼠和叙利亚仓鼠PrP23 - 144淀粉样纤维的连续主链和侧链碳和氮归属。所归属的化学位移用于预测小鼠和叙利亚仓鼠PrP23 - 144淀粉样蛋白核心区域的二级结构，并将结果与先前已通过固态核磁共振技术分析的人类PrP23 - 144淀粉样蛋白的结果进行比较。
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