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. 2019 Mar 26;294(19):7740–7754. doi: 10.1074/jbc.RA118.007347

Table 1.

List of mathematical model parameters

The table and the meaning of the parameters have been previously published by Liepe et al. (11), and they correspond to the parameters indicated in Fig. 1A.

Peptide-bond hydrolysis
    kp Peptide-bond hydrolysis rate at active site(s)
    KaS, KaP Dissociation constant of substrate (S) and product (P) to active site(s)
    na Hill coefficient for binding to active site(s)
    KiS and KiP Dissociation constant of substrate (S) and product (P) to inhibitor site(s)
    ni Hill coefficient for binding to inhibitor site(s)
    α Factor, by which KaS, KaP, KiS, and KiP are multiplied
    β Factor, by which kp is multiplied upon binding to inhibitory site(s)
Transport
    kon Association rate to the gate
    koff Dissociation rate to from gate
    vin Peptide influx rate
    τ Peptide translocation rate inside the chamber
    vout Peptide efflux rate
    C Capacity (maximum number of molecules inside the chamber)
Transport regulation
    Ron Binding rate to the enhancing regulator site(s)
    Roff Unbinding rate to the enhancing regulator site(s)
    Xenh Strength of enhancing regulator site(s)
    Ion Binding rate to the inhibiting regulator site(s) outside the chamber
    Ioff Unbinding rate to the inhibiting regulator site(s) outside the chamber
    H Coefficient for binding to inhibiting regulator site(s) outside the chamber
    Yin Strength of inhibiting regulator site(s)