Solid-state NMR backbone chemical shift assignments of α-synuclein amyloid fibrils at fast MAS regime

IF 0.8 4区生物学 Q4 BIOPHYSICS

Biomolecular NMR Assignments Pub Date : 2024-06-29 DOI:10.1007/s12104-024-10186-2

Zigmantas Toleikis, Piotr Paluch, Ewelina Kuc, Jana Petkus, Darius Sulskis, Mai-Liis Org-Tago, Ago Samoson, Vytautas Smirnovas, Jan Stanek, Alons Lends

引用次数: 0

Abstract

The α-synuclein (α-syn) amyloid fibrils are involved in various neurogenerative diseases. Solid-state NMR (ssNMR) has been showed as a powerful tool to study α-syn aggregates. Here, we report the ¹H, ¹³C and ¹⁵N back-bone chemical shifts of a new α-syn polymorph obtained using proton-detected ssNMR spectroscopy under fast (95 kHz) magic-angle spinning conditions. The manual chemical shift assignments were cross-validated using FLYA algorithm. The secondary structural elements of α-syn fibrils were calculated using ¹³C chemical shift differences and TALOS software.

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快速 MAS 机制下 α-突触核蛋白淀粉样纤维的固态 NMR 主干化学位移分配。

α-突触核蛋白（α-syn）淀粉样纤维与多种神经退行性疾病有关。固态核磁共振（ssNMR）已被证明是研究α-syn聚集体的有力工具。在此，我们报告了在快速（95 kHz）魔角旋光条件下使用质子检测的 ssNMR 光谱获得的一种新的α-syn 多晶体的 1H、13C 和 15N 骨背化学位移。使用 FLYA 算法对手动化学位移分配进行了交叉验证。利用 13C 化学位移差异和 TALOS 软件计算了 α-syn 纤维的二级结构元素。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Biomolecular NMR Assignments 生物-光谱学

CiteScore

1.70

自引率

11.10%

发文量

审稿时长

6-12 weeks

期刊介绍： Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.