Publication: Universal structure in the relaxation of photoactive proteins
Universal structure in the relaxation of photoactive proteins
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Janke, P., Dorbath, E., Stock, G., & Hamm, P. (2025). Universal structure in the relaxation of photoactive proteins. Journal of Chemical Physics, 163, 210902. https://doi.org/10.1063/5.0299435
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Abstract
The nonequilibrium relaxation of a series of, in part, very different photoactive proteins is compared, ranging over up to eleven decades in time. The series comprises various PDZ domains and MCL 1/peptide complexes with artificial azobenzene photoswitches, as well as two different cyanobacteriochromes (Slr-g3 and TePixJ). In either case, an embedded chromophore photoisomerizes after electronic excitation on an ultrafast femtosecond to picosecond timescale, initially perturbing the structure of the protein directly around the chromoph
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Janke, P., Dorbath, E., Stock, G., & Hamm, P. (2025). Universal structure in the relaxation of photoactive proteins. Journal of Chemical Physics, 163, 210902. https://doi.org/10.1063/5.0299435