Jove
Visualize
お問い合わせ
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

関連する概念動画

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.2K
2.2K
Protein-protein Interfaces02:04

Protein-protein Interfaces

15.0K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
15.0K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.6K
4.6K
Protein Networks02:26

Protein Networks

4.7K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.7K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

9.4K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
9.4K

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

A genome-wide CRISPR screen defines host determinants of early <i>Brucella</i> infection in human macrophage-like cells.

Infection and immunity·2026
Same author

Cell polarity control by an unconventional G-protein complex in bacteria.

Nature communications·2026
Same author

Bacterial cell division protein FtsZ complexes with a phage protein to activate bacterial immunity.

Nature microbiology·2026
Same author

A genome-wide CRISPR screen defines host determinants of early <i>Brucella</i> infection in human macrophage-like cells.

bioRxiv : the preprint server for biology·2026
Same author

Unmasking pathogen traits for chronic colonization in neurogenic bladder.

Cell reports·2026
Same author

DefensePredictor: A machine learning model to discover prokaryotic immune systems.

Science (New York, N.Y.)·2026

関連する実験動画

Updated: Mar 31, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.7K

新しいタンパク質-タンパク質相互作用特異性を,乱交的中間物質によって進化させる.

Christopher D Aakre1, Julien Herrou2, Tuyen N Phung1

  • 1Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

Cell
|October 20, 2015
PubMed
まとめ
この要約は機械生成です。

タンパク質の進化はしばしば共進化を伴うが,新しいモデルでは,乱交的な中間体が特異性の変化を促進することを示唆している. この研究は,細菌の毒素-抗毒素系における相互作用が進化の多様化を可能にする方法を示しています.

さらに関連する動画

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.8K
Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

6.6K

関連する実験動画

Last Updated: Mar 31, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.7K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.8K
Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

6.6K

科学分野:

  • 進化生物学
  • 分子生物学
  • 生物化学

背景:

  • 共同進化するアミノ酸は,タンパク質の相互作用特異性にとって重要な残基を特定することができます.
  • 伝統的なモデルでは,インターフェースの変異が補償的な変化を誘導し,非機能的な中間物質を必要とします.
  • 代替モデルでは,最初は特異性を拡大し,その後はパートナーに適応することを提案しています.

研究 の 目的:

  • タンパク質の共同進化の代替モデルを調査する.
  • 相互作用の特異性の進化のための乱交性ベースのモデルの妥当性を実証する.
  • タンパク質ファミリーの多様化における乱交変異の役割を探求する.

主な方法:

  • バクテリアの毒素-抗毒素系における インターフェース変異体の大きな図書館をスクリーニングする.
  • 特定の変異と乱交変異の間の接続を特定するためにシーケンス空間を分析する.
  • タンパク質の相互作用の進化を研究するためのモデルとして,細菌の毒素-抗毒素システムを利用する.

主要な成果:

  • 毒素と抗毒素の乱雑な変種は,相互作用の特異性を再プログラムするための中間物質として機能します.
  • 高特異性の毒素と抗毒素は,配列空間において,より乱交的な形態と結びついている.
  • この研究は 進化的変化のための 乱交に基づくモデルの実現可能性を示しています

結論:

  • 混沌としたタンパク質の変種は相互作用特異性の進化を容易にする.
  • 毒素対毒素システムの多様化を促しています
  • このモデルは,パラログのタンパク質ファミリーの進化に関する新しい視点を提供します.