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

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Mutations in Microorganisms01:18

Mutations in Microorganisms

Mutations are heritable changes in an organism’s genome involving alterations in the base sequence of DNA or RNA. These changes can influence cellular processes and phenotypic traits, potentially transforming the unaltered wild type into a mutant form. Such changes, termed forward mutations, are pivotal in shaping the genetic diversity of organisms.RNA viruses exhibit the highest mutation rates due to the absence of robust proofreading mechanisms during genome replication. In contrast,...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

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

Tubulin State Determines Proteopathic Fate.

Cytoskeleton (Hoboken, N.J.)·2026
Same author

Modulation of Biomolecular Aggregate Morphology and Condensate Infectivity.

Biomolecules·2026
Same author

NANOG Proximity Proteomics Maps Neighborhood Hubs Linked to Mesenchymal Stem Cell Stemness and Chromatin Control.

Biomolecules·2026
Same author

Condensate State as Determinant of Amyloid Pathology in Neurodegeneration.

Biomolecules·2026
Same author

Multivalent weak contacts shape chaperone-nascent protein interactions.

bioRxiv : the preprint server for biology·2026
Same author

Label-Free Microfluidic Modulation Spectroscopy Monitors RNA Origami Structure and Stability.

Biosensors·2026

関連する実験動画

Updated: Jun 23, 2026

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates
11:49

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates

Published on: August 21, 2018

結合親近性の変異によって引き起こされる変化におけるアンサンブル変調の役割を特徴づける.

Anthony Manson1, Steven T Whitten, Josephine C Ferreon

  • 1Department of Biochemistry and Molecular Biology, and Sealy Center for Structural Biology and Biophysics, University of Texas Medical Branch, Galveston, Texas 77555, USA.

Journal of the American Chemical Society
|April 29, 2009
PubMed
まとめ

タンパク質の構成的変動は,分子認識のような生物学的機能にとって極めて重要です. 私たちの研究は,これらのダイナミクスを,特にSH3ドメインで分析すると,結合エネルギーが正確に予測され,タンパク質-リガンド相互作用の洞察が明らかになることを示しています.

さらに関連する動画

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

関連する実験動画

Last Updated: Jun 23, 2026

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates
11:49

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates

Published on: August 21, 2018

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

科学分野:

  • タンパク質のダイナミクス
  • 分子認識による分子認識
  • バイオフィジックス 生物物理学

背景:

  • タンパク質の構成変動は,生物学的プロセスにとって不可欠である.
  • これらのダイナミクスを理解することは,酵素触媒,分子認識,およびアロステリックシグナル伝達を理解するのに役立ちます.

研究 の 目的:

  • サブストラット/リガンドの認識における構造変動の役割を調査する.
  • SH3ドメインとそのパートナーペプチドの間の結合反応を分析する.

主な方法:

  • 硬球衝突モデルのアルゴリズムを使用して,SH3ドメインの変動を計算した.
  • 構造に基づくエネルギー関数による計算された結合エネルギー.
  • 構成変化を特徴付けるために,計算された集合に主要な座標分析を適用した.

主要な成果:

  • シンプルなモデルでは,SH3結合エネルギーに対する変異効果を正確に再現した.
  • SH3の順位変動,特にRTループは多様で,ランダム状態で近似されます.
  • 変異体間の結合親和の差異は,形状の変化の主なモードの変化と相関する.

結論:

  • ダイナミックなタンパク質ループは,幅広い構成状態にアクセスできます.
  • 分子認識の包括的な理解には,タンパク質状態の完全な分布を考慮する必要がある.
  • このアプローチは,タンパク質-リガンドの相互作用に関する定量的な洞察を提供します.