Formation of homo-dimer R2

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Two ScbR (R) proteins bind together to form an ScbR homo-dimer (R2).

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Chemical equation

2R \rightleftharpoons R_{2}

Rate equation

 r= \frac{k^{-}_{6}}{K_{d6}}\cdot [R]^{2} - k^{-}_{6}\cdot [R_{2}]

Parameters

The parameters of this reaction are the dissociation constant for binding of one ScbR to another (K_{d6}) and the dissociation rate for binding of one ScbR to another (k^{-}_{6}).

Name Value Units Origin Remarks
K_{d6} 35.3 [1]  nM Studies with Streptomyces DnaA Protein
k^{-}_{6} 10^{-3} [2] [3]  min^{-1} Strong protein-protein interactions rate constants

Parameters with uncertainty

The probability distributions, adjusted accordingly in order to reflect the above values, are the following:

The most plausible parameter value for the K_{d6} is decided to be  35 nM and the confidence interval  100 . This means that the mode of the PDF is 35 and the range where 95% of the values are found is between 0.1 and 10^{3} nM .

In a similar way, the most plausible value for k^{-}_{6} is 10^{-3} min^{-1} and the confidence interval 10. This means that the mode of the PDF is 10^{-3} and the range where 95% of the values are found is between 10^{-4} and 10^{-2} min^{-1}.

The probability distributions for the two parameters, adjusted accordingly in order to reflect the above values, are the following:

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The location and scale parameters of the distributions are:

Parameter μ σ
K_{d6} 4.4804 1.4757
k^{-}_{6} -6.0926 0.9028

References

  1. Majka J, Zakrzewska-Czerwiñska J, Messer W. Sequence recognition, cooperative interaction, and dimerization of the initiator protein DnaA of Streptomyces. J Biol Chem. 2001;276(9):6243-52.
  2. Wesley E. Stites. Protein−Protein Interactions:  Interface Structure, Binding Thermodynamics, and Mutational Analysis. Chemical Reviews 1997 97 (5), 1233-1250
  3. Janin, Joel. The kinetics of protein-protein recognition. Proteins-Structure Function and Bioinformatics (1997): 153-161.