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

Ligand Binding Sites02:40

Ligand Binding Sites

14.2K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
14.2K
Conserved Binding Sites01:49

Conserved Binding Sites

4.7K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.7K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.2K
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...
8.2K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.0K
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...
14.0K
Induced-fit Model01:13

Induced-fit Model

85.4K
Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
85.4K
Protein Folding01:25

Protein Folding

9.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
9.7K

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

Editorial: Molecular modeling in drug repurposing.

Frontiers in molecular biosciences·2026
Same author

Evolutionary diversity and structural dynamics of the outer membrane protein Ail in <i>Yersinia</i>.

Journal of biomolecular structure & dynamics·2026
Same author

Exploring the structure and dynamics of peptide nanodiscs through a synergistic approach with NMR spectroscopy, SAS and MD simulations.

Communications chemistry·2026
Same author

Structure-Based Experimental Datasets for Benchmarking Protein Simulation Force Fields [Article v1.0].

Living journal of computational molecular science·2026
Same author

Antimicrobial peptides at (lipid) interfaces: Insights from monolayer models.

Advances in colloid and interface science·2026
Same author

The Martini 3 Lipidome: Expanded and Refined Parameters Improve Lipid Phase Behavior.

ACS central science·2025

関連する実験動画

Updated: Oct 22, 2025

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.2K

リピド-タンパク質結合における逆適合性選択

Amélie Bacle1, Pavel Buslaev2,3, Rebeca Garcia-Fandino4,5

  • 1Laboratoire Coopératif "Lipotoxicity and Channelopathies - ConicMeds", Université de Poitiers, 1 rue Georges Bonnet, Poitiers 86000, France.

Journal of the American Chemical Society
|September 1, 2021
PubMed
まとめ

脂質のヘッドグループには いくつかの固い構造ではなく 幅広い形状があります この構造的柔軟性により,脂質はタンパク質,RNA,薬剤を含む様々なバイオ分子に効果的に結合できます.

さらに関連する動画

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

2.1K
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

7.4K

関連する実験動画

Last Updated: Oct 22, 2025

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.2K
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

2.1K
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

7.4K

科学分野:

  • バイオ化学とナノバイオテクノロジー
  • 分子生物物理学

背景:

  • 膜とナノ粒子の脂質ヘッドグループは,バイオ分子との相互作用を媒介する.
  • ナノバイオテクノロジー (例えば,mRNAワクチンの媒介者) のような分野では,脂質のヘッドグループ構成を理解することは極めて重要です.
  • 以前の研究では,生理学的条件下における脂質ヘッドグループ構成組の実験データがなかった.

研究 の 目的:

  • 重要な脂質群の構成組を生物学的条件で決定する.
  • 脂質ヘッドグループがいくつかの硬い構造を採用するか,連続した形状のスペクトルを採用するかどうかを調査する.
  • バイオ分子相互作用に対する脂質ヘッドグループの柔軟性の意味を探求する.

主な方法:

  • 固体核磁共振 (NMR) 実験と分子動力学 (MD) シミュレーションの組み合わせ (NMRリピッドプロジェクト)
  • 様々な条件下で4つの主要な脂質を分析した.
  • タンパク質データバンク (PDB) から894のタンパク質に結合した脂質構造を調べた.

主要な成果:

  • 脂質ヘッドグループは,中性および有電荷の膜の構造の幅広く重なり合っています.
  • ヘッドグループ化学は形状の確率分布に影響を与えます 範囲自体ではありません
  • 脂質は,ヘッドグループ化学に関係なく,様々な形状のタンパク質に結合する.

結論:

  • 脂質ヘッドグループは,広範な形状の柔軟性を持っています.
  • 脂質は,この柔軟性を利用して,様々なタンパク質に結合するための適切な形状を選択します.
  • 提案された逆形状選択モデルは,タンパク質,薬物,RNA,ウイルスとの脂質相互作用に適用されます.