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Updated: Apr 5, 2026

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST
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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST

Published on: November 2, 2018

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分子ステップリングとNMRによるアロステリックセンサにおける州特有の関連定数の測定

Kody J Moleschi1, Madoka Akimoto1, Giuseppe Melacini1

  • 1Department of Chemistry and Chemical Biology, and ‡Department of Biochemistry and Biomedical Sciences, McMaster University , 1280 Main Street West, Hamilton, Ontario L8S 4M1, Canada.

Journal of the American Chemical Society
|August 7, 2015
PubMed
まとめ

研究者は,アロステリックセンサーにおける州特有の結合親和性を測定するための新しい方法を開発した. このテクニックは,サイクルアデノシンモノフォスファート (cAMP) 依存タンパク質キナーゼ (PKA-RIα) の親和性の差異は,主にエフェクター選択性ではなく,ダイナミックな均衡シフトによるものであることを明らかにした.

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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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