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. 2001 May 15;98(11):6003–6008. doi: 10.1073/pnas.101571298

Figure 1.

Figure 1

Phosphorylation kinetics of wild-type CheY by PAM. Reactions were performed in the absence of peptide (○), the presence of 1 mM FliM peptide (□), the presence of 1 mM CheZ peptide (⋄), the presence of 15 μM CheA-P2 (▵), or the presence of 1 mM CheZ205VE peptide (×). Measurements were done with a stopped-flow instrument, and constant ionic strength was maintained. Observed first-order rate constants (kobs) were determined from individual phosphorylation time courses at the indicated phosphodonor concentrations. For clarity, kobs values obtained in the absence of peptide (○) and in the presence of CheA-P2 (▵) are replotted in Inset with a different y-axis scale.