Conformation change fluorescence lifetime studies

In conclusion, TIRF promises to be exceedingly useful in the study of protein-substrate interactions. It gives in situ, possibly remote, real-time information about protein adsorption-desorption parameters, conformational changes upon adsorption and hopefully, nanosecond time-resolved fluorescence lifetime information about adsorbed proteins 156). 

Fluorescence lifetimes of melamine-formaldehyde resins have been measured and concluded not to be important in the photodegradation of the resins.Circular dichroism studies on -polyCl phenyl-azobenzoyl-L-lysine) have shown that conformational changes are... 

The emission characteristics of fluorophores (the quantum yield and the wavelength of the emission maximum) are sensitive to their immediate environment and this leads to pronounced changes of fluorescence during protein denaturation (16). The high sensitivity of fluorescence to environmental effects was demonstrated in a particularly effective way in a study in which the decay of tryptophan fluorescence was followed in a number of proteins containing a single tryptophan residue (17). Deviations from simple exponential decay were interpreted as demonstrating that these proteins have a variable conformations, with the rate of their interconversion slow compared with the lifetime of the excited tryptophan. 

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