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. 2021 Dec 29;17(12):e1009756. doi: 10.1371/journal.pcbi.1009756

Table 1. Model Parameters.

Parameter Brief description Value Source
Dc Diffusion constant for the TolB-Pal complex 0.0068 μm2s-1 Our fitting
Db Diffusion constant for free TolB 0.0036 μm2s-1 Our fitting
Df Diffusion constant for free Pal Equal to Dc We assume that the limiting factor for diffusion is the embedding of Pal’s lipoylated domain in the outer membrane, similar to how the mobility of membrane proteins is determined by the number of transmembrane domains[19]
ɑ Rate of binding of TolB and Pal 0.054 μM-1s-1 [17]
β0 Rate the TolB-Pal complex is pulled apart by TolQRA 17 s-1 Our fitting
ɣ Rate the TolB-Pal complex dissociates 0.006 s-1 [17]
kon Rate Pal binds to the peptidoglycan 0.1 μM-1s-1 Estimate
koff Rate Pal unbinds peptidoglycan 1.0 s-1 Estimate
T Concentration of peptidoglycan binding sites 320 μM Found from the height difference of the valley of the effective diffusion coefficient
σ Standard deviation of the truncated normal distribution for the shape of TolQRA in dividing cells 0.08 Found from fitting to the shape of the valley in the effective diffusion coefficient