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. Author manuscript; available in PMC: 2009 Jan 11.
Published in final edited form as: J Mol Biol. 2007 Oct 22;375(2):581–594. doi: 10.1016/j.jmb.2007.10.044

Figure 4.

Figure 4

Determination of Kop and kopen from observed rate constants plotted versus trypsin concentration. A) Over a wide range of concentrations the data can be described by a hyperbola. Under opening-limited conditions kexp approaches a fixed limit: these plots are fit to the full kinetic equation (Equation 7), giving Kop and kopen values. Data shown is for dimer at 37°C. B) In cleavage-limiting conditions, plots of kexp are linear with respect to enzyme, with a slope of Kop·kcat/KM. Data shown is for capsid at 37°C.