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Capturing Protein Dynamics with Time Resolved Luminescence Spectroscopy

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Figure 1.2: We measure ruthenium-heme electron tunneling rates in cytochromecb562 following photoexcitation of [Ru(bpy)2(IA-phen)]2+ complexes that have beencovalently attached at various positions in the protein.
Figure 1.3:Time-resolved fluorescence energy transfer:analysis and results for a solution containing compact, intermediate, and extendedprotein conformations
Figure 1.4: Dansyl fluorophore used in FRET studies.
Figure 3.3: Representative electrospray ionization mass spectrum of Ru-labeledcytochrome cb562 (variant K19C).
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