用于魔角旋转固态核磁共振光谱的淀粉样纤维的制备
Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.
作者信息
Tuttle Marcus D, Courtney Joseph M, Barclay Alexander M, Rienstra Chad M
机构信息
Department of Chemistry, University of Illinois at Urbana-Champaign, A129B CLSL, Box 50-6, 600 South Mathews Avenue, Urbana, IL, 61801, USA.
Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.
出版信息
Methods Mol Biol. 2016;1345:173-83. doi: 10.1007/978-1-4939-2978-8_11.
Solid-state NMR spectroscopy (SSNMR) is an established and invaluable tool for the study of amyloid fibril structure with atomic-level detail. Optimization of the homogeneity and concentration of fibrils enhances the resolution and sensitivity of SSNMR spectra. Here, we present a fibrillization and fibril processing protocol, starting from purified monomeric α-synuclein, that enables the collection of high-resolution SSNMR spectra suitable for site-specific structural analysis. This protocol does not rely on any special features of α-synuclein and should be generalizable to any other amyloid protein.
固态核磁共振光谱（SSNMR）是一种成熟且极为重要的工具，可用于在原子水平细节上研究淀粉样纤维结构。优化纤维的均匀性和浓度可提高SSNMR光谱的分辨率和灵敏度。在此，我们提出了一种从纯化的单体α-突触核蛋白开始的纤维化和纤维处理方案，该方案能够收集适用于位点特异性结构分析的高分辨率SSNMR光谱。此方案不依赖于α-突触核蛋白的任何特殊特性，并且应该可以推广到任何其他淀粉样蛋白。
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