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. Author manuscript; available in PMC: 2008 Apr 13.
Published in final edited form as: Mol Cell. 2007 Apr 13;26(1):27–39. doi: 10.1016/j.molcel.2007.02.020

Figure 1.

Figure 1

The linker stimulates the ATPase activity of the isolated ATPase domain, similar to the effect of substrate on full-length DnaK. (A) Steady-state ATPase rates measured at pH 7.6. (B) pH-dependence of steady-state ATPase activities for full-length wild-type DnaK in the absence (△) and presence (▲) of p5 peptide, DnaK(1-388) (○), and DnaK(1-392) (●). Error bars represent standard deviation from ≥3 experiments.