Difference between revisions of "Formation of homo-dimer R2"

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[[Image:Kd6-text.png|center|thumb|700px|Majka et al. 2001<ref name="Majka2001"></ref>]]
 
[[Image:Kd6-text.png|center|thumb|700px|Majka et al. 2001<ref name="Majka2001"></ref>]]
  
These values agree with Ozbabacan et al. <ref name="Saliha2011"> [http://peds.oxfordjournals.org/content/early/2011/06/15/protein.gzr025.full.pdf 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]</ref> who state that strong protein-protein interactions such as homodimerization have equilibrium dissociation constants <math> \less 10^{-6} M</math> and mostly in the nanomolar range.
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These values agree with Ozbabacan et al. <ref name="Saliha2011"> [http://peds.oxfordjournals.org/content/early/2011/06/15/protein.gzr025.full.pdf 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]</ref> who state that strong protein-protein interactions such as homodimerization have equilibrium dissociation constants <math> < 10^{-6} M</math> and mostly in the nanomolar range.
 
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|<math>k^{-}_{6}</math>
 
|<math>k^{-}_{6}</math>

Revision as of 19:14, 15 October 2015

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 Value in previous GBL models Remarks-Reference
K_{d6} 35.3-114 [1] nM N/A Majka et al. published a study on dimerization of the initiator Protein DnaA of Streptomyces and on its mutants, where they report dissociation constants in the range 35.3-114 nM.
Majka et al. 2001[1]

These values agree with Ozbabacan et al. [2] who state that strong protein-protein interactions such as homodimerization have equilibrium dissociation constants  < 10^{-6} M and mostly in the nanomolar range.

k^{-}_{6} 60-6 \cdot 10^{4} [3] [4] min^{-1} N/A According to Northrup et al. the K_{a} of protein-protein bond formations occur in the order of 10^{6} M^{-1}s^{-1}. Therefore, this value is used to calculate the dissociation rate for the ScbR homo-dimer formation. Therefore the range of the k^{-}_{3} values is calculated as per k^{-}_{6}=K_{d6} \cdot K_{a}.
Northrup et al. 1992[4]

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} 5.7331 1.4757
k^{-}_{6} -6.0926 0.9028

References