These pages illustrate aspects of fluorescence spectroscopy that are useful for elucidating structural and dynamic properties of proteins. Fluorescent techniques can provide parameters consistent with crystallographic results. The various environments of the fluorophores of a folded protein and the unique stereochemistry of the polypeptide chain affect the fluorophores in many ways which can be used to characterize and to follow changes in the folded conformation in solution. Fluorescence-based techniques can give information about a protein's conformation, binding sites, solvent interactions, degree of flexibility, internal motions, rotational diffusion coefficient, and many other physicochemical parameters.
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