Jove
Visualize
お問い合わせ

関連する概念動画

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

20.7K
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...
20.7K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.4K
15.4K
Forces Acting on Chromosomes02:11

Forces Acting on Chromosomes

4.1K
During mitosis, chromosome movements occur through the interplay of multiple piconewton level forces. In prometaphase, these forces help in chromosome assembly or congression at the equatorial plane, eventually leading to their alignment at the metaphase plate. The forces acting on the chromosomes are space and time-dependent; therefore, they vary with the position of the chromosomes as the cell progresses through mitosis. 
Microtubules and motor proteins exert two types of forces on...
4.1K
Forces Acting on Chromosomes02:11

Forces Acting on Chromosomes

1.9K
1.9K
The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

3.9K
The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...
3.9K
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

4.4K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
4.4K

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

Label-free DNA structural profiling via elliptical dichroism spectroscopy.

Biosensors & bioelectronics·2026
Same author

Hydrogen-deuterium exchange points to inter-domain interactions in reverse gyrase that modulate conformational changes in positive DNA supercoiling.

The Journal of biological chemistry·2026
Same author

Structural basis of chaperone mechanisms in cells and the evolutionary emergence of the protein world.

bioRxiv : the preprint server for biology·2026
Same author

NMR-based conformational analysis of DNA G-quadruplex guides mapping essential structure-function relationship in protein chaperoning.

Physical chemistry chemical physics : PCCP·2026
Same author

Self-Assembling RNA Nanostructures are Highly Sensitive to Environmental Conditions.

Journal of molecular biology·2025
Same author

Catalyzing Protein Folding by Chaperones.

Biology·2025
Same journal

Co-option of lysosomal machinery shapes the evolution of the intracellular photosymbiosis supporting coral reefs.

Cell·2026
Same journal

LEF1 and niche factors determine T cell stemness across chronic diseases.

Cell·2026
Same journal

Recurrent patterns of TOP1-mediated neuronal genomic damage shared by major neurodegenerative disorders.

Cell·2026
Same journal

Four-dimensional molecular mapping from a spatial snapshot reveals the dynamics of hair follicle organogenesis.

Cell·2026
Same journal

Whole-cell particle-based digital twin simulations from 4D lattice light-sheet microscopy data.

Cell·2026
Same journal

Systematic discovery of pathogen effector functions across human pathogens and pathways.

Cell·2026
関連記事をすべて見る
JoVE
x logofacebook logolinkedin logoyoutube logo
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 JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する実験動画

Updated: Mar 19, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

3.4K

シェパローンの行動の原動力

Philipp Koldewey1, Frederick Stull1, Scott Horowitz1

  • 1Department of Molecular, Cellular and Developmental Biology, and the Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109, USA.

Cell
|June 14, 2016
PubMed
まとめ
この要約は機械生成です。

Spyのような分子チャペロンは Im7のようなクライアントタンパク質を 結合し折りたたむために 液体性相互作用だけでなく 静電力を使います このメカニズムは 特殊な指示なしに 様々なタンパク質の折りたたみを支援します

さらに関連する動画

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

11.1K
In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

7.5K

関連する実験動画

Last Updated: Mar 19, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

3.4K
Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

11.1K
In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

7.5K

科学分野:

  • 分子生物学
  • バイオ物理学
  • タンパク質の折りたたみ

背景:

  • プロテインの折り畳みを制御する精密な分子力は,まだ完全に理解されていません.
  • チャペロンは タンパク質の折りたたみを支援し 結合や誤折りを防止する 重要な細胞機構です

研究 の 目的:

  • シャーロンとクライアントの相互作用の4つの重要なステップである結合,安定化,折り畳み,放出を駆動する分子力の詳細なメカニズム的理解を明らかにする.
  • チャペロンは主に水害性相互作用によって展開されたタンパク質を認識するという一般的な考えに異議を唱える.

主な方法:

  • モデルシャプロンスパイと その開いたクライアントタンパク質 Im7を調査した.
  • Chaperone-clientの相互作用の異なる段階を分析し,それぞれのステップに関与する力に焦点を当てました.

主要な成果:

  • 一般的な考えに反して,Spy chaperoneは,開いた Im7 クライアントタンパク質への初期急速な結合のために,長距離の静電相互作用を使用します.
  • 短距離の水性相互作用は,シャパロン-クライアント複合体を安定させ,その後,水性崩壊がクライアントタンパク質の折りたたみを引き起こします.
  • クライアントタンパク質の折りたたみにより,水害性の残留物を埋めて,Spyの親和性を減らし,放出を促進し,自己折りたたみを可能にします.

結論:

  • Spy Chaperoneは,静電相互作用によって開始されるメカニズムを採用し,その後,水害性安定化とクライアント主導の折り畳みにより,放出につながります.
  • クライアントタンパク質が自己折りたたむことを可能にするこのチャペロンメカニズムは,様々な無関係のタンパク質に対するチャペロンの広範な基板特異性を説明する可能性がある.