Studies of tryptophan fluorescence using bacteriophage T4 lysozyme

摘要

The nature of the complex fluorescence of the indole chromophore of tryptophan is briefly reviewed. A recent molecular dynamics simulation of the relaxation of water surrounding the excited state of tryptophan demonstrates that this 'dielectric relaxation' aspect of tryptophan photophysics is well-understood. The relationship of this behavior in solutions to the photophysics of tryptophan in proteins is discussed. Another well-known feature of tryptophan fluorescence is the ability of a variety of 'collisional quenchers' to reduce the emission yield and lifetime. The relevance of this aspect of the photophysics of tryptophan to protein luminescence is also discussed.