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Updated: Jul 11, 2026

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
10:44

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Published on: October 21, 2016

无NO结合的肌球蛋白:NO连接体的结构多样性和动态

Tomasz Zemojtel1, Matteo Rini, Karsten Heyne

  • 1Department of Bioinformatics, University of Wuerzburg, Am Hubland, D-97074 Wuerzburg, Germany. zemojtel@biozentrum.uni-wuerzburg.de

Journal of the American Chemical Society
|February 20, 2004
PubMed
概括

氧化 (NO) 在光解后迅速与肌球蛋白重组. 这种二原子连接体在蛋白质内明显倾斜,探索各种结合位置.

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Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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