The Beck group uses femtosecond nonlinear spectroscopy to study photophysical and photochemical processes in photosynthetic light-harvesting proteins, photosynthetic reaction centers, and model systems.

The current focus is on how carotenoids function in energy transfer and photoprotection mechanisms in light-harvesting proteins. We are working now on how intramolecular charge transfer enables peridinin to function as a mid-visible light-harvesting chromophore in the peridinin–chlorophyll protein from dinoflagellates.

A second project examines the control of energy- and electron-transfer processes in chromoproteins by dynamic solvation, the reorganizational motions of the protein structure that occur in response to the formation of electronic excited states. This area now focuses on how the hydration shell of water molecules that surrounds a protein is coupled to protein motions.

Both research areas exploit femtosecond two-dimensional photon-echo and transient-grating spectroscopies with Fourier-transform, spectral interferometry detection to characterize the formation and decay of electronic coherences and to discern the motion of the surrounding protein or solvent medium.


The Beck laboratory acknowledges new support from the DOE/BES Photosynthetic Systems program (award DE-SC0010847).