関連する実験動画

Updated: Jun 27, 2026

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

協力的な分子認識インターフェースにおける部分結合状態の証拠

Elena Chekmeneva1, Christopher A Hunter, Martin J Packer

  • 1Department of Chemistry, University of Sheffield, Sheffield S3 7HF, and AstraZeneca, Alderley Park, Cheshire SK10 4TG, United Kingdom.

Journal of the American Chemical Society
|December 10, 2008
PubMed
まとめ

本研究では,亜鉛ポルフィリン受容体とピリジンリガンドを用いた協同的多点結合を調査しています. 結合の安定性は,水素結合の強さと溶媒の極性に依存し,複合体の形成に影響する.

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Noncovalent Attractions in Biomolecules

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Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Noncovalent Attractions in Biomolecules02:35

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Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
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Cooperative Allosteric Transitions01:58

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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...
Cooperative Allosteric Transitions01:58

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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...