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関連する概念動画

Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

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 polypeptide...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

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関連する実験動画

Updated: Jun 5, 2026

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

複雑な分子認識インターフェースの解剖

Christopher A Hunter1, Maria Cristina Misuraca, Simon M Turega

  • 1Department of Chemistry, University of Sheffield, Sheffield S3 7HF, United Kingdom. c.hunter@sheffield.ac.uk

Journal of the American Chemical Society
|December 23, 2010
PubMed
まとめ
この要約は機械生成です。

この研究は,超分子複合体における分子内水素結合を定量化しています. 結果は,これらの結合が添加的であり,その有効性は,単に幾何学ではなく,化学的構造に依存していることを示しています.

さらに関連する動画

Hand Controlled Manipulation of Single Molecules via a Scanning Probe Microscope with a 3D Virtual Reality Interface
11:00

Hand Controlled Manipulation of Single Molecules via a Scanning Probe Microscope with a 3D Virtual Reality Interface

Published on: October 2, 2016

関連する実験動画

Last Updated: Jun 5, 2026

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

Hand Controlled Manipulation of Single Molecules via a Scanning Probe Microscope with a 3D Virtual Reality Interface
11:00

Hand Controlled Manipulation of Single Molecules via a Scanning Probe Microscope with a 3D Virtual Reality Interface

Published on: October 2, 2016

科学分野:

  • 超分子化学 超分子化学
  • 化学生物学 化学生物学とは
  • 物理化学 物理化学

背景:

  • 超分子複合体は,非共性相互作用によって形成される.
  • 水素結合は,分子認識と自己組織化において重要な役割を果たします.
  • 個々の相互作用の定量的な貢献を理解することは,複雑な分子システムの設計の鍵です.

研究 の 目的:

  • 亜鉛・ポルフィリン・ピリジン・スーパモレキュラー複合体の一連の合成と特徴を特定し,分子内水素結合の数を変化させる.
  • 単一の水素結合がこれらの複合体の全体的な安定性と組成に与える貢献を定量的に評価する.
  • 複雑な分子認識インターフェースにおける分子構造,水素結合,および協力性の関係を調査する.

主な方法:

  • 周辺の水素結合群を持つ亜鉛ポルフィリンおよびピリジンリガンドの合成.
  • 自動紫外線/紫外線タイトリングで120種類の異なる超分子複合体を特徴付けます.
  • 分子内水素結合相互作用と有効モラリティ (EM) を定量化するために化学の二重変異サイクルを構築する.

主要な成果:

  • 単一の水素結合の自由エネルギー貢献は加算であり,超分子構造との差異はほとんどない.
  • 幾何学的に不可能である場合,分子内水素結合は存在しない;優れた互補性は高い親和性を保証しない.
  • 分子内カルボキシラートエステル-フェノールH結合 (200 mM) の有効なモラリティは,フォスフォナートダイエステル-フェノールH結合 (30 mM) よりも数桁高い.

結論:

  • この研究では,分子内水素結合は加法性であり,組み立てへの影響は建築から大きく独立していることが明らかになりました.
  • 幾何学的な補完性だけでは高い結合親和性を決定するものではなく,形状の柔軟性は有効なモラリティに限られた影響を及ぼします.
  • H-ボンドの種類間の有効なモラリティの有意な差異は,より強いボンドがより厳格な幾何学的な制約を課し,形成効率に影響を与える,補償効果を示唆しています.