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Updated: Jun 5, 2025

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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在单体前纤维状状态下可视化高斯链状的人类α-synuclein的结构模型:解决方案SAXS数据和建模分析分析

Madhumita Dey1, Arpit Gupta1, Maulik D Badmalia1

  • 1CSIR - Institute of Microbial Technology, Chandigarh, India.

International journal of biological macromolecules
|December 14, 2024
PubMed
概括

这项研究可视化了使用小角度X射线散射的α-synuclein的前纤维单体状态. 结果表明,形状的形状是无序的,最好用曲的模型来表示,其α-螺旋含量较低.

关键词:
在ALPHAFOLD2中使用.欧盟组织组织 (EOM)一个单体的单体.正常模式分析正常模式分析蛋白质结构 蛋白质结构萨克斯 (SAXS) 的时间.α-Synuclein 是一种蛋白质.

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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