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. Author manuscript; available in PMC: 2010 Aug 2.
Published in final edited form as: Biochemistry. 2006 Aug 1;45(30):9074–9084. doi: 10.1021/bi060567d

Figure 6.

Figure 6

Kinetics of mant-ATP dissociation from unphosphorylated wild-type PKR measured by stopped-flow fluorescence spectroscopy. Time-dependent changes in fluorescence of 40 μM mant-ATP in the presence of 1 μM unphosphorylated PKR competed off with 2 mM ATP. The mixture was excited at 295 nm and fluorescence emission above 400 nm measured using a cutoff filter. The plot represents average of 21 runs with each run made of 1000 data points taken over 10 s in a log time interval. The solid line is the two exponential fits to the data. The first phase contributed 94% to the total amplitude with rate constant (kobs,1) of 175 ± 2 s−1 while the second phase contributed 6% to the total amplitude with kobs,2 of 43.1 ± 5.5 s−1.