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This process is experimental and the keywords may be updated as the learning algorithm improves. These keywords were added by machine and not by the authors. Additionally, fluorophores often display spectral shifts when they bind to membranes. Alternatively, the ligand may induce a spectral shift in the intrinsic or extrinsic protein fluorescence. Binding is usually accompanied by a spectral shift due to the different environment for the bound ligand. Suppose a fluorescent ligand binds to a protein. However, there are many additional instances where solvent effects are used. 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. One common use of solvent effects is to determine the polarity of the probe binding site on the macromolecule. 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. These effects are the origin of the Stokes’ shift, which is one of the earliest observations in fluorescence. Solvent polarity and the local environment have profound effects on the emission spectra of polar fluorophores.