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Structural dynamics in photoswitchable fluorescent proteins:

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Light harvesting in photosynthetic systems involves excitation energy transfer on ultrafast timescales. Any photosynthetic system adapts to varying sunlight conditions through photoswitching. Photoswitching involves photoinduced slow (micro- to milli-seconds) conformational changes that result in switching between bright and dark states. Such light induced conformational changes were shown to occur within photosynthetic pigment-protein complexes as well as within fluorescent proteins. We wish to map the potential energy surface (PES) across the family of fluorescent proteins and study structural dynamics in photoswitchable/photoactivable fluorescent proteins.

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How slow processes (conformational changes) affect the ultrafast processes ?

What is the molecular-level mechanism of photosynthetic (or rather, photoprotective) role of FPs?

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See our recent work on excited state dynamics of a yellow fluorescent protein variant:

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