Binding of R2 to A

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The ScbR homo-dimer (R2) forms a complex with ScbA (A).

Chemical equation

A + R_{2} \rightleftharpoons A-R_{2}

Rate equation

 r= \frac{k^{-}_{3}}{K_{d3}}\cdot [A]\cdot [R_{2}] - k^{-}_{3}\cdot [A-R_{2}]

Parameters

The parameters of this reaction are the dissociation constant for binding of ScbR to ScbA (K_{d3}) and the dissociation rate for binding of ScbR to ScbA (k^{-}_{3}). Since no evidence of the existence of the ScbA-ScbR complex has been found so far, our belief is that the interaction between the two proteins should be an unstable/ transient. The values of such complexes according to the literature [1] , lie in the millimolar or micromolar scale.

Protein Interaction-2011.png

Parameter Value Units Origin Remarks
K_{d3} 10^{3} - 10^{9} [2] nM Comparison of strong vs weak protein-protein interactions Range of values that correspond to weak protein interactions
k^{-}_{3} 0.6-1.2 min^{-1} [2] [3] min^{-1} Generalistic mechanisms of protein-protein interaction

Parameters with uncertainty

The most plausible parameter values and the confidence interval were decided to be:

K_{d3} = 10^{3} \pm 10 nM

k^{-}_{3}= 0.9 \pm 0.3 min^{-1}

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

References

  1. Saliha Ece Acuner Ozbabacan, Hatice Billur Engin, Attila Gursoy, and Ozlem Keskin. Transient protein–protein interactions. Protein Engineering, Design and Selection first published online June 15, 2011
  2. 2.0 2.1 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 Genetics 28.2 (1997): 153-161.