Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved in...

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers.

Frontiers in neuroscience·2021
Same author

Parallel and Sequential Pathways of Molecular Recognition of a Tandem-Repeat Protein and Its Intrinsically Disordered Binding Partner.

Biomolecules·2021
Same author

ThX - a next-generation probe for the early detection of amyloid aggregates.

Chemical science·2021
Same author

Machine learning-aided protein identification from multidimensional signatures.

Lab on a chip·2021
Same author

Distinct responses of human peripheral blood cells to different misfolded protein oligomers.

Immunology·2021
Same author

Comparative Studies in the A30P and A53T α-Synuclein <i>C. elegans</i> Strains to Investigate the Molecular Origins of Parkinson's Disease.

Frontiers in cell and developmental biology·2021

相关实验视频

Updated: Jul 19, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

使用自旋标记NMR和集成分子动力学模拟来绘制α-synuclein中的远程相互作用.

Matthew M Dedmon1, Kresten Lindorff-Larsen, John Christodoulou

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

Journal of the American Chemical Society
|January 13, 2005
PubMed
概括

帕金森病涉及阿尔法-同核蛋白蛋白. 它的原生结构,部分凝结,可以防止有毒聚合物的形成,为帕金森病提供新的治疗点.

更多相关视频

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One &#945;-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

相关实验视频

Last Updated: Jul 19, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One &#945;-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

科学领域:

  • 生物化学 生物化学
  • 神经科学是一个神经科学.
  • 蛋白质化学 蛋白质化学

背景情况:

  • 阿尔法-同核素本质上是无序的,并且是帕金森病病源的核心.
  • 蛋白质聚合是像帕金森氏症这样的神经退行性疾病的标志.

研究的目的:

  • 为了研究alpha-synuclein的本土结构组合.
  • 了解alpha-synuclein在帕金森病中的作用的结构基础.

主要方法:

  • 水力动力半径测量.
  • 蛋白质序列和电荷分布的分析.

主要成果:

  • 原生α-synuclein存在于符合者的分布中,而不是随机的线圈.
  • 观察到一个部分凝结的结构,小于一个随机的线圈.
  • 这种结构是由C端电荷和中心疏水区域相互作用引起的.

结论:

  • 阿尔法-同核素的原生,部分凝结结构可能会抑制毒性聚合.
  • 这一发现为帕金森病提供了潜在的新治疗策略.