Search research articles

お問い合わせ

JoVEについて

概要リーダーシップブログ JoVEヘルプセンター

著者向け

出版プロセス編集委員会範囲と方針査読よくある質問投稿

図書館員向け

推薦の声購読アクセスリソース図書館諮問委員会よくある質問

研究

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments アーカイブ

教育

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual 教員リソースセンター教員サイト

プライバシーポリシー

関連する概念動画

Cryo-electron Microscopy

Cryo-electron Microscopy

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...

Electron Microscope Tomography and Single-particle Reconstruction

Electron Microscope Tomography and Single-particle Reconstruction

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...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

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...

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え

Same author

Impact of a brief peri-operative counselling session on parental awareness of passive smoking in paediatric ambulatory surgery: A single-centre observational study.

European journal of anaesthesiology and intensive care·2026

Same author

In situ architecture of plasmodesmata in Physcomitrium patens resolved by cryo-electron tomography.

Nature plants·2026

Same author

Structural basis of membrane potential coupled vectorial CO₂ hydration by the DAB2 complex in chemolithoautotrophs.

Nature communications·2026

Same author

Impact of a Multidisciplinary Algorithm on Early Complications After Hip Fracture Surgery: A Retrospective Time-Series Study.

Anesthesia and analgesia·2026

Same author

Hemodynamic effects of plain versus hyperbaric bupivacaine during spinal anesthesia for total knee arthroplasty: a randomized clinical trial.

Regional anesthesia and pain medicine·2026

Same author

Structural remodeling of the mitochondrial protein biogenesis machinery under proteostatic stress.

Science advances·2026

Same journal

Six ways to put the public at the heart of science and policy.

Nature·2026

Same journal

The complex truth about trust in science.

Nature·2026

Same journal

Have people stopped trusting science? The data tell a surprising story.

Nature·2026

Same journal

How FAIR data are helping to build trust in science.

Nature·2026

Same journal

Scientists should recognize their own political biases to build public trust.

Nature·2026

Same journal

Harmonizing standards and resources for the medical genome.

Nature·2026

関連記事をすべて見る

Search research articles

関連する実験動画

Updated: Jun 15, 2025

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

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

Published on: November 20, 2021

冷凍電子トモグラフィによるチャペロニン機能の視覚化

Jonathan Wagner^1,2,3,4, Alonso I Carvajal¹, Andreas Bracher¹

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

|August 21, 2024

まとめ

この要約は機械生成です。

GroELやGroESのようなチャペロニンは細胞内のタンパク質の折り畳みを促進しますこの研究では,これらの複合体を in situで視覚化し,その本来のサイクルとクライアントタンパク質の結合と折り畳みを明らかにします.

さらに関連する動画

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

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

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

Published on: January 30, 2016

関連する実験動画

Last Updated: Jun 15, 2025

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

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

Published on: November 20, 2021

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

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

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

Published on: January 30, 2016

科学分野:

分子生物学
構造生物学
細胞生物学

背景:

チャペロニンはタンパク質の折りたたみを支援する重要な分子機構です
バクテリアのシャペロニンGroELは,そのコファクターGroESと共に,タンパク質の折りたたみのためのケージのような構造を形成する.
以前の研究では,チャペロニンの機能を理解するために,in vitroの分析に頼っていた.

研究の目的:

GroEL,GroES,およびクライアントタンパク質の機能的ステキオメトリーを in situ で決定する.
自然な細胞環境でチャペロニン複合体を視覚化するために
バクテリアのチャペロニンの本来の反応サイクルを解明する.

主な方法:

細胞内のシャペロニン複合体を視覚化するために,冷凍電子トモグラフィーを使用した.
チャペロニン複合体の形状を定量的に分析した.
高解像度構造を in vitro で検証した.

主要な成果:

GroEL複合体の約55-70%はGroESを非対称的に結合し,残りの部分は対称である.
サブストラットタンパク質は非対称複合体の自由環に存在し,サブストラット受容状態を示す.
GroEL-GroES室内での放出前にカプセル化された基板タンパク質が折りたたまれた状態で観察されました.

結論:

タンパク質の折りたたみに関する非対称的および対称的な副反応を含む反応サイクルが提案された.
この研究は,細胞内のネイティブの構成および機能的なチャペロニンサイクルを直接可視化します.
発見は,チャペロニンが介在するATP依存タンパク質の in vivoメカニズムを明らかにする.