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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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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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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Allosteric Regulation01:08

Allosteric Regulation

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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...
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Ligand Binding and Linkage

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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...
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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...
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ナノシートに対するアロステリック・モジュレーション

Hao Deng1,2,3,4, Ying Wang3, Yanqiu Lu2

  • 1Department Joint School of National University of Singapore and Tianjin University, International Campus of Tianjin University Binhai New City 350207 Fuzhou, China.

Journal of the American Chemical Society
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まとめ
この要約は機械生成です。

高品質のノンイオン共性有機フレームワークナノシート (nCOFNs) の合成のためのアロステリック調節戦略を開発しました. この方法は,高度な膜アプリケーションのための優れた溶液処理性を持つnCOFNの温和な環境合成を可能にします.

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科学分野:

  • 材料科学
  • ナノテクノロジー
  • 超分子化学

背景:

  • ノニオニック共性有機フレームワークナノシート (nCOFN) は有望な構成要素ですが,溶液で合成することは困難です.
  • 高品質のnCOFN合成には,層内および層間相互作用の制御が不可欠である.
  • 生物学的調節メカニズムであるアロステリーは,COFのような合成材料で探索されていません.

研究 の 目的:

  • β-ケトエナミン結合 nCOFNsの溶液相合成のためのアロステリック調節戦略を導入する.
  • nCOFNアセンブリを制御するアロステル変調剤としての二次アミンの役割を調査する.
  • 温和な条件下でnCOFNで高結晶性と大きな面比を達成する.

主な方法:

  • 二次アミンをアロステル変調剤として使用し,エノル・ケトー分極化とステル阻害を制御した.
  • バランスの取れたアロステリック効果のための最適化された調節特性 (N暴露,副群サイズ).
  • nCOFNの合成のために使用された穏やかな環境条件.

主要な成果:

  • 結晶度が高く,面比が1000以上で,高品質のnCOFNを合成した.
  • 温和な環境下では高い収穫率 (82%まで) を得ている.
  • 超高メタノール浸透率 (127 L m−2 h−1 bar−1) の膜に組み立てられる優れた溶液処理性を実証した.

結論:

  • アロステル調節戦略は,高度なnCOFNを合成するための新しいアプローチを提供します.
  • 合成されたnCOFNsは,耐久性および製薬浄化を含む膜アプリケーションで優れた性能を示す.
  • 大面積のフラットシートと空洞の繊維膜の製造によって実証された実用的な応用可能性.