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Updated: Jul 18, 2026

Optical Control of a Neuronal Protein Using a Genetically Encoded Unnatural Amino Acid in Neurons
08:20

Optical Control of a Neuronal Protein Using a Genetically Encoded Unnatural Amino Acid in Neurons

Published on: March 28, 2016

金属誘発サイクリングによるオリゴヌクレオチド混合化のアロステル制御

Mareike Göritz1, Roland Krämer

  • 1Anorganisch-Chemisches Institut, Universität Heidelberg, Im Neuenheimer Feld 270, 69120 Heidelberg, Germany.

Journal of the American Chemical Society
|December 22, 2005
PubMed
まとめ

DNAサイクルは,鉄によるリング閉塞によって形成されます. 亜鉛イオンは,特定の濃度範囲内で補完的なDNA結合を制御するユニークなアロステリック効果を誘発します.

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Allosteric Regulation

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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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Regulation of Metabolism

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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...