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相关概念视频

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

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Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
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Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

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Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
Electron tomography can be performed either in TEM or STEM (scanning transmission...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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相关实验视频

Updated: Jun 15, 2025

Preparation and Cryo-FIB micromachining of Saccharomyces cerevisiae for Cryo-Electron Tomography
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Preparation and Cryo-FIB micromachining of Saccharomyces cerevisiae for Cryo-Electron Tomography

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通过冷电子断层扫描在现场可视化沙佩罗宁功能

Jonathan Wagner1,2,3,4, Alonso I Carvajal1, Andreas Bracher1

  • 1Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.

Nature
|August 21, 2024
PubMed
概括
此摘要是机器生成的。

像GroEL和GroES这样的Chaperonin促进细胞内的蛋白质折叠. 这项研究可视化了这些复合体,揭示了它们的本源循环以及它们如何结合和折叠客户端蛋白质.

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Using Tomoauto: A Protocol for High-throughput Automated Cryo-electron Tomography
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科学领域:

  • 分子生物学
  • 结构生物学
  • 细胞生物学

背景情况:

  • 链是有助于蛋白质折叠的重要分子机器.
  • 细菌的陪伴剂GroEL及其辅助因子GroES形成了一个类似子的蛋白质折叠结构.
  • 之前的研究依赖于体外分析来了解沙佩罗宁的功能.

研究的目的:

  • 在现场确定GroEL,GroES和客户端蛋白的功能静脉测量.
  • 在自然的细胞环境中可视化沙佩罗宁复合体.
  • 为了阐明细菌的原生反应周期.

主要方法:

  • 使用冷电子断层扫描可视化细胞内的沙佩罗宁复合体.
  • 进行了对Chaperonin复合体形状的定量分析.
  • 在试验室中获得的高分辨率结构被用于验证.

主要成果:

  • 大约55-70%的GroEL复合物以不对称的方式结合GroES,其余部分是对称的.
  • 基质蛋白在不对称复合体的自由环上发现,表明基质接受状态.
  • 在释放之前,在GroEL-GroES室内观察到封装基质蛋白质的折叠状态.

结论:

  • 为蛋白质折叠提出了一种涉及连接不对称和对称子反应的反应循环.
  • 这项研究直接可视化了细胞内的原生形状和功能性沙佩罗宁循环.
  • 这些发现揭示了由沙佩罗宁介导的ATP依赖蛋白质折叠的体内机制.