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Updated: Feb 20, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
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分子子CLR01稳定了一个无序的蛋白质-蛋白质接口

David Bier1,2, Sumit Mittal3, Kenny Bravo-Rodriguez3

  • 1Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology , Den Dolech 2, 5612 AZ Eindhoven, The Netherlands.

Journal of the American Chemical Society
|October 18, 2017
PubMed
概括

这项研究表明,分子针CLR01通过结合无序识别动机和刚性适配蛋白来稳定蛋白质相互作用 (PPI),从而增强结合亲和力.

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相关概念视频

Protein-Protein Interfaces02:04

Protein-Protein Interfaces

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Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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