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Solvent Effects on Emission Spectra

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Principles of Fluorescence Spectroscopy

Abstract

Solvent polarity and the local environment have profound effects on the emission spectra of polar fluorophores. These effects are the origin of the Stokes’ shift, which is one of the earliest observations in fluorescence. Emission spectra are easily measured, and as a result, there are numerous publications on emission spectra of fluorophores in different solvents and when bound to proteins, membranes, and nucleic acids. One common use of solvent effects is to determine the polarity of the probe binding site on the macromolecule. This is accomplished by comparison of the emission spectra and/or quantum yields of the fluorophore when it is bound to the macromolecule and when it is dissolved in solvents of different polarity. However, there are many additional instances where solvent effects are used. Suppose a fluorescent ligand binds to a protein. Binding is usually accompanied by a spectral shift due to the different environment for the bound ligand. Alternatively, the ligand may induce a spectral shift in the intrinsic or extrinsic protein fluorescence. Additionally, fluorophores often display spectral shifts when they bind to membranes.

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Lakowicz, J.R. (1999). Solvent Effects on Emission Spectra. In: Principles of Fluorescence Spectroscopy. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-3061-6_6

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  • DOI: https://doi.org/10.1007/978-1-4757-3061-6_6

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