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

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(Parameters)
(Parameters)
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|<math>k^{-}_{6}</math>
 
|<math>k^{-}_{6}</math>
|<math>60-6 \cdot 10^{4}</math> <ref name="Janin1997"> [http://onlinelibrary.wiley.com/doi/10.1002/(SICI)1097-0134(199706)28:2%3C153::AID-PROT4%3E3.0.CO;2-G/epdf Janin, Joel. ''The kinetics of protein-protein recognition.'' Proteins-Structure Function and Bioinformatics (1997): 153-161.]</ref> <ref name="Northrup1992"> [http://www.pnas.org/content/89/8/3338.full.pdf Northrup S.H. and Erickson H.P. ''Kinetics of protein-protein association explained by Brownian dynamics computer simulation.''PNAS 1992;89(8),3338-3342]</ref>
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|<math>2.12-6.84</math> <ref name="Janin1997"> [http://onlinelibrary.wiley.com/doi/10.1002/(SICI)1097-0134(199706)28:2%3C153::AID-PROT4%3E3.0.CO;2-G/epdf Janin, Joel. ''The kinetics of protein-protein recognition.'' Proteins-Structure Function and Bioinformatics (1997): 153-161.]</ref> <ref name="Northrup1992"> [http://www.pnas.org/content/89/8/3338.full.pdf Northrup S.H. and Erickson H.P. ''Kinetics of protein-protein association explained by Brownian dynamics computer simulation.''PNAS 1992;89(8),3338-3342]</ref>
 
|<math>min^{-1}</math>
 
|<math>min^{-1}</math>
 
| N/A
 
| N/A
|According to Northrup et al. the <math>K_{a}</math> of protein-protein bond formations occur in the order of <math>10^{6} M^{-1}s^{-1}</math>. Therefore, this value is used to calculate the dissociation rate for the ScbR homo-dimer formation. Therefore the range of the <math>k^{-}_{3}</math> values is calculated as per <math>k^{-}_{6}=K_{d6} \cdot K_{a}</math>.
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|According to Northrup et al. the <math>K_{a}</math> of protein-protein bond formations occur in the order of <math>10^{6} M^{-1}s^{-1}</math>. Therefore, this value is used to calculate the dissociation rate for the ScbR homo-dimer formation. Therefore the range of the <math>k^{-}_{3}</math> values is <math>2.12-6.84 min^{-1}</math>, calculated as per <math>k^{-}_{6}=K_{d6} \cdot K_{a}</math>.
 
[[Image:K3-text.png|center|thumb|350px|Northrup et al. 1992<ref name="Northrup1992"></ref>]]
 
[[Image:K3-text.png|center|thumb|350px|Northrup et al. 1992<ref name="Northrup1992"></ref>]]
 
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Revision as of 19:25, 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} 2.12-6.84 [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 2.12-6.84 min^{-1}, 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