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Fluorescence spectroscopy is an ideal and powerful methodology for the potent and reliable study of protein-ligand interactions. Enhanced susceptibility accompanied with comparative easiness forms the prominent key factor for the application of fluorescence techniques in these studies. In fluorescence technique, protein-ligand interactions are often studied at very low concentrations compared to other optical methods with a thousandfold higher sensitivity. In this method, we measure the variation in quantum yield upon ligand binding, by observing variations in ligand fluorescence, intrinsic protein fluorescence, or fluorescence of covalently or noncovalently bound fluorescent probes that are sensitive to ligand binding. Sensitivity of a fluorescent ligand to the environment, energy transfer from protein to ligand producing reduction in protein fluorescence or amplification of ligand fluorescence, a conformational change in protein/ ligand on binding to the protein, etc., contribute to the changes in quantum yield upon ligand binding [1–3]. This chapter will outline a sketch of steady-state fluorescence techniques for defining molecular interactions and calculation of binding constants.

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PublisherData powered by TypesetSpringer, Singapore
Open AccessNo