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

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|<math>10^{-3}</math> <ref name="Stites1997"> Wesley E. Stites. ''Protein−Protein Interactions:  Interface Structure, Binding Thermodynamics, and Mutational Analysis.'' Chemical Reviews 1997 97 (5), 1233-1250</ref> <ref name="Janin1997"> Janin, Joel. ''The kinetics of protein-protein recognition.'' Proteins-Structure Function and Bioinformatics (1997): 153-161.</ref>
 
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Revision as of 02:50, 5 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 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

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.