Photophysics of ANS V. decay modes of ANS in proteins: The IFABP–ANS complex Original Research Article

The fluorescence properties of ANS as bound to proteins are treated. Several points of view concerning the origin of these properties are reviewed and synthesized into one framework. On proteins where the quantum yield (QY) is appreciable, as in organic solvents, the preferred conformation of ANS is often with the phenyl ring nearly (65°–85°) orthogonal to the naphthalene. The major consequence of this geometry is water exclusion from the critical zone of ANS at which the largest amount of solvent dipolar relaxation originates. This, in turn, leads to a depression of the rate of electron transfer to the surroundings, together with other effects, as noted in the literature and in our lab. Alternative quenching pathways for ANS on the protein vs in water are also elucidated.