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関連する概念動画

Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence 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...

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関連する実験動画

Updated: Jun 28, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

タンパク質におけるアロステリック制御の設計のための表面部位.

Jeeyeon Lee1, Madhusudan Natarajan, Vishal C Nashine

  • 1Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.

Science (New York, N.Y.)
|October 18, 2008
PubMed
まとめ
この要約は機械生成です。

科学者たちは,光感知ドメインを酵素と結びつけることで,新しいタンパク質,PAS-DHFRを設計しました. これにより,光に反応する制御可能なタンパク質が生成され,タンパク質工学の新しい方法が示されます.

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Modeling an Enzyme Active Site using Molecular Visualization Freeware
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Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

関連する実験動画

Last Updated: Jun 28, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Modeling an Enzyme Active Site using Molecular Visualization Freeware
14:37

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

科学分野:

  • バイオケミストリー バイオケミストリー
  • プロテイン工学は,タンパク質の
  • 分子生物学は分子生物学である.

背景:

  • タンパク質ファミリーは,遠隔の機能的表面を結びつける共進化するアミノ酸ネットワークを示しています.
  • これらのネットワークは,分子内ネットワークに加わり,タンパク質にアロステリック制御をエンジニアリングするための戦略を示唆しています.

研究 の 目的:

  • チメリックタンパク質を作成することによって,エンジニアリングアロステリック制御のコンセプトをテストする.
  • 信号ドメインを酵素に接続することによって,タンパク質の活性が調節できることを示すために.

主な方法:

  • 共同進化するアミノ酸ネットワークを特定するために,タンパク質ファミリーの統計分析.
  • 植物性Per/Arnt/Sim (PAS) 信号ドメインとEscherichia coliの二酸化葉酸還元酵素 (DHFR) を融合させ,キメリックタンパク質 (PAS-DHFR) の設計と作成.

主要な成果:

  • 設計されたPAS-DHFRキメリックタンパク質は,最適化なしで光に依存した触媒活性を示した.
  • 観測された光に依存する活動は,特定の結合部位と,両方の親タンパク質の既知のシグナル伝達機構に依存していた.

結論:

  • PAS-DHFRは,タンパク質に制御機能を組み込むための概念証明の役割を果たします.
  • 保存されたアロステリック部位でのインターフェース設計は,タンパク質に新しい規制活動を生み出すための実行可能な戦略です.