The control of protein structure and function with light has numerous applications in biology.
Naturally occurring light sensitive proteins such as channel rhodopsins and LOV domains can be harnessed to provide optical control of processes ranging from neuronal excitability and protein-protein interactions. These naturally occurring proteins can sometimes be mutated/selected to have altered photochemical behavior (colour, lifetime), but the ranges of behavior are often somewhat limited.
We have explored the direct development of photochemical switches for which the photochemical properties can be rationally tuned (wavelength, thermal relaxation rate, degree of conformational change). Our efforts have focused on the well studied chromophore azobenzene for which can be covalent coupling to proteins has been shown to drive functional changes.
This chemical-biological approach provides a complementary strategy for the development of photo-controlled proteins that can be advantageous for cases where detailed structural data are available for a target protein.