Fig. 7: Steady-state kinetics of mANTP binding to OaPAC. | Communications Biology

Fig. 7: Steady-state kinetics of mANTP binding to OaPAC.

From: ATP-dependent conformational dynamics in a photoactivated adenylate cyclase revealed by fluorescence spectroscopy and small-angle X-ray scattering

Fig. 7: Steady-state kinetics of mANTP binding to OaPAC.The alternative text for this image may have been generated using AI.

(i) Time-dependent changes in fluorescence intensity of the mantATP upon binding to OaPAC measured by stopped-flow fluorescence spectroscopy (mantATP concentrations; black line: 10 μΜ, orange line: 15μΜ μΜ, blue line 20μΜ, cyan line: 40 μΜ, brown line: 50 μΜ) (ii) Plot of the rate constants (kobs) determined versus the mantATP concentration. Fitting of the data to a double exponential allows determination of both the association and the dissociation rate constant for mantATP from OaPAC.

Back to article page