Fig. 1: Schematics of photodissociation.
From: Simulation-guided engineering of split GFPs with efficient β-strand photodissociation
a Scheme of photodissociation and strand-exchange experiments. The protein is cleaved between strand 10 and 11 and irradiated with a 488 nm laser, causing excitation, isomerization, and dissociation of the original strand 10 in the presence of excess synthetic strands containing T203Y. Upon binding, the synthetic strand shifts the absorption from green to yellow, enabling measurement of pseudo-first order exchange rates that reflect the rate of photodissociation. b Detailed view highlighting the N and C termini, internal alpha helix (gray), chromophore, the beta-strands 7 (purple), 10 (green/yellow), and 11 (blue), and the modeled loops on both ends of strand 11 (red). Scissors indicate the proteolytic cleavage site. c Schematic of potential energy curves for photodissociation (black lines7), overlaid with the computational methods used to model the states (dots). The excited and ground states are degenerate at the conical intersection (red).
